match no.target idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
1COG46373739699.72.2E-17[                               ----------------  ]COG4637Predicted ATPase
2COG49383746599.61.2E-14[                                 ----------      ]COG4938Predicted ATPase
3COG11063716799.31.2E-11[                                -----------      ]AAA15ATPase/GTPase, AAA15 family
4COG39504404599.33.5E-11[------                                           ]COG3950Predicted ATP-binding protein involved in virulence
5pfam133041445599.21.5E-10[                                   --------      ]AAA_21AAA domain.
6COG35935817999.21.3E-10[                                 ------------    ]YbjDPredicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains
7pfam131753447299.23.1E-10[                                -----------      ]AAA_15AAA ATPase domain. This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.
8COG11202587499.21.5E-10[                                 -------------   ]FepCABC-type cobalamin/Fe3+-siderophores transport system, ATPase component
9cd032252117299.16.9E-10[                                 ------------    ]ABC_cobalt_CbiO_domain1First domain of the ATP-binding cassette component of cobalt transport system. Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
10cd032141807499.04.3E-09[                                 -------------   ]ABC_Iron-Siderophores_B12_HeminATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins. ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
11COG11312937799.09.1E-09[                                 -------------   ]CcmAABC-type multidrug transport system, ATPase component
12cd032642117598.97.6E-09[                                 -------------   ]ABC_drug_resistance_likeABC-type multidrug transport system, ATPase component. The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
13cd032262057398.91.1E-08[                                 ------------    ]ABC_cobalt_CbiO_domain2Second domain of the ATP-binding cassette component of cobalt transport system. Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
14cd032192367498.92.4E-08[                                 -------------   ]ABC_Mj1267_LivG_branchedATP-binding cassette component of branched chain amino acids transport system. The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
15cd032602277698.96.2E-08[                                  ------------   ]ABC_PstB_phosphate_transporterATP-binding cassette domain of the phosphate transport system. Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
16cd032402046598.93.5E-08[                                 ----------      ]ABC_Rad50ATP-binding cassette domain of Rad50. The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
17COG11222357498.91.4E-08[                                 -------------   ]EcfA2Energy-coupling factor transporter ATP-binding protein EcfA2
18COG11953638898.86.6E-08[                                --------------   ]RecFRecombinational DNA repair ATPase RecF
19cd032301737198.83.1E-08[                                  -----------    ]ABC_DR_subfamily_AATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A. This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
20PRK000643618398.88.6E-08[                                 ------------    ]recFrecombination protein F; Reviewed
21cd032352136898.76.8E-08[                                 ------------    ]ABC_Metallic_CationsATP-binding cassette domain of the metal-type transporters. This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
22cd032622137098.71.4E-07[                                  -----------    ]ABC_HisP_GlnQATP-binding cassette domain of the histidine and glutamine transporters. HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
23COG39102335398.62.7E-07[                                      --------   ]COG3910Predicted ATPase
24TIGR006113654598.65E-07[------                                           ]recfrecF protein. All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
25cd032781974398.62.8E-07[------                                           ]ABC_SMC_barmotinATP-binding cassette domain of barmotin, a member of the SMC protein family. Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
26COG11212548198.61.3E-07[                                 --------------  ]ZnuCABC-type Mn2+/Zn2+ transport system, ATPase component
27COG45552457598.67.4E-07[                                  ------------   ]NatAABC-type Na+ transport system, ATPase component NatA
28COG11262407298.67.5E-07[                                  ------------   ]GlnQABC-type polar amino acid transport system, ATPase component
29COG04112507098.61.7E-07[                                  -----------    ]LivGABC-type branched-chain amino acid transport system, ATPase component
30cd032242227398.59.3E-07[                                  ------------   ]ABC_TM1139_LivF_branchedATP-binding cassette domain of branched-chain amino acid transporter. LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
31cd032692107598.52.9E-07[                                 -------------   ]ABC_putative_ATPaseATP-binding cassette domain of an uncharacterized transporter. This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
32cd032562417598.52.5E-06[                                 -------------   ]ABC_PhnC_transporterATP-binding cassette domain of the binding protein-dependent phosphonate transport system. Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
33TIGR011661905898.52.2E-07[                                 ----------      ]cbiOcobalt transport protein ATP-binding subunit. This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux.
34COG11172535798.51.2E-06[                                  ---------      ]PstBABC-type phosphate transport system, ATPase component
35cd032632207698.59.6E-07[                                 -------------   ]ABC_subfamily_AATP-binding cassette domain of the lipid transporters, subfamily A. The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
36cd032452207198.51.9E-06[                                  ------------   ]ABCC_bacteriocin_exportersATP-binding cassette domain of bacteriocin exporters, subfamily C. Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
37TIGR009722477398.52.5E-06[                                  ------------   ]3a0107s01c2phosphate ABC transporter, ATP-binding protein. This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters.
38cd032722436298.49.3E-07[                                 ----------      ]ABC_SMC3_eukATP-binding cassette domain of eukaryotic SMC3 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
39TIGR045212778198.43.2E-06[                                  -------------- ]ECF_ATPase_2energy-coupling factor transporter ATPase. Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes.
40pfam134762034098.41.7E-07[------                                           ]AAA_23AAA domain.
41cd032662187598.43.8E-06[                                 -------------   ]ABC_NatA_sodium_exporterATP-binding cassette domain of the Na+ transporter. NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
42cd032612357498.43.6E-06[                                 -------------   ]ABC_Org_Solvent_ResistantATP-binding cassette transport system involved in resistant to organic solvents. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
43cd032422707798.44.2E-06[                                  -----------    ]ABC_RecFATP-binding cassette domain of RecF. RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
44TIGR035223017598.31E-06[                                 -------------   ]GldA_ABC_ATPgliding motility-associated ABC transporter ATP-binding subunit GldA. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
45PRK112642507398.36.5E-06[                                  ------------   ]PRK11264putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
46COG04102377598.33.8E-06[                                  ------------   ]LivFABC-type branched-chain amino acid transport system, ATPase component
47COG36382587598.36.9E-06[                                 -------------   ]PhnCABC-type phosphate/phosphonate transport system, ATPase component
48PRK106192577298.31.4E-05[                                  ------------   ]PRK10619histidine/lysine/arginine/ornithine transporter subunit; Provisional
49pfam13555604398.38.9E-07[------                                           ]AAA_29P-loop containing region of AAA domain.
50cd032682087498.35.7E-06[                                 -------------   ]ABC_BcrA_bacitracin_resistATP-binding cassette domain of the bacitracin-resistance transporter. The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
51COG04199084498.35.5E-07[------                                           ]SbcCDNA repair exonuclease SbcCD ATPase subunit
52cd032291786998.36E-06[                                  -----------    ]ABC_Class3ATP-binding cassette domain of the binding protein-dependent transport systems. This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
53PRK112312557498.31.8E-05[                                 -------------   ]fecEiron-dicitrate transporter ATP-binding subunit; Provisional
54COG46042527598.33.6E-06[                                 -------------   ]CeuDABC-type enterochelin transport system, ATPase component
55PRK142643057498.31.1E-05[                                  ------------   ]PRK14264phosphate ABC transporter ATP-binding protein; Provisional
56PRK136472747498.29.8E-07[                                 -------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
57COG11272637498.21.7E-05[                                 -------------   ]MlaFABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF
58PRK094932407498.21.5E-05[                                  ------------   ]glnQglutamine ABC transporter ATP-binding protein; Reviewed
59pfam113983734598.28.6E-06[------                                           ]DUF2813Protein of unknown function (DUF2813). This entry contains YjbD from Escherichia coli, which is annotated as a nucleotide triphosphate hydrolase.
60PRK135392075898.26.2E-06[                                 ----------      ]PRK13539cytochrome c biogenesis protein CcmA; Provisional
61TIGR034112427298.22.3E-05[                                  -----------    ]urea_trans_UrtDurea ABC transporter, ATP-binding protein UrtD. Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity.
62cd032572287598.22.6E-05[                                 -------------   ]ABC_NikE_OppD_transportersATP-binding cassette domain of nickel/oligopeptides specific transporters. The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
63COG41612427498.23.1E-05[                                  ------------   ]ArtPABC-type arginine transport system, ATPase component
64COG03962517398.23.9E-05[                                  ------------   ]SufCFe-S cluster assembly ATPase SufC
65cd032672367498.12E-05[                                 ------------    ]ABC_NatA_likeATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA. NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
66pfam0246311624298.11.5E-06[------                                           ]SMC_NRecF/RecN/SMC N terminal domain. This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolizm and recombination.
67PRK142542857598.11.5E-05[                                  ------------   ]PRK14254phosphate ABC transporter ATP-binding protein; Provisional
68TIGR038732567498.11.1E-05[                                 -------------   ]F420-0_ABC_ATPproposed F420-0 ABC transporter, ATP-binding protein. This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
69COG45863257698.12.3E-05[                                 -------------   ]COG4586ABC-type uncharacterized transport system, ATPase component
70PRK111242427498.13.2E-05[                                  ------------   ]artParginine transporter ATP-binding subunit; Provisional
71TIGR0216911644498.11.4E-06[------                                           ]SMC_prok_Achromosome segregation protein SMC, primarily archaeal type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent.
72COG45982567298.10.00013[                                  ------------   ]HisPABC-type histidine transport system, ATPase component
73PRK136513057298.11.1E-05[                                  ------------   ]PRK13651cobalt transporter ATP-binding subunit; Provisional
74cd032752474498.12E-06[------                                           ]ABC_SMC1_eukATP-binding cassette domain of eukaryotic SMC1 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
75TIGR033756947298.12.7E-05[                                  ------------   ]type_I_sec_LssBtype I secretion system ATPase, LssB family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export.
76COG11183457798.14.2E-05[                                 -------------   ]CysAABC-type sulfate/molybdate transport systems, ATPase component
77COG119611634698.13.2E-06[------                                           ]SmcChromosome segregation ATPase
78COG11362267398.16.8E-05[                                 -------------   ]LolDABC-type lipoprotein export system, ATPase component
79TIGR045202688298.18.3E-05[                                 --------------- ]ECF_ATPase_1energy-coupling factor transporter ATPase. Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes.
80TIGR023152437598.05.9E-05[                                 -------------   ]ABC_phnCphosphonate ABC transporter, ATP-binding protein. Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates.
81PRK136392758398.02.5E-06[                                 --------------- ]cbiOcobalt transporter ATP-binding subunit; Provisional
82PRK039188804398.04.9E-06[------                                           ]PRK03918chromosome segregation protein; Provisional
83COG28842237298.05.6E-05[                                  ------------   ]FtsEABC-type ATPase involved in cell division
84cd032592137698.05.6E-05[                                 -------------   ]ABC_Carb_Solutes_likeATP-binding cassette domain of the carbohydrate and solute transporters-like. This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
85cd032391784398.01.8E-06[------                                           ]ABC_SMC_headThe SMC head domain belongs to the ATP-binding cassette superfamily. The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
86PRK136362837498.05.4E-06[                                 -------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
87COG11242527698.09.4E-05[                                 -------------   ]DppFABC-type dipeptide/oligopeptide/nickel transport system, ATPase component
88cd032552187398.00.00012[                                 ------------    ]ABC_MJ0796_LolCDE_FtsEATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
89TIGR0216811794398.07E-06[------                                           ]SMC_prok_Bchromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle.
90PRK142472507098.03.6E-05[                               ------------      ]PRK14247phosphate ABC transporter ATP-binding protein; Provisional
91PRK135482588198.09.6E-05[                                 -------------   ]hmuVhemin importer ATP-binding subunit; Provisional
92COG11353397597.98E-05[                                 -------------   ]AbcCABC-type methionine transport system, ATPase component
93PRK142442517697.90.00017[                                  ------------   ]PRK14244phosphate ABC transporter ATP-binding protein; Provisional
94COG49885597297.99.7E-05[                                  ------------   ]CydDABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components
95cd032742124597.91.1E-05[------                                           ]ABC_SMC4_eukATP-binding cassette domain of eukaryotic SMC4 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
96cd032712616697.90.00025[                                 ----------      ]ABC_UvrA_IIATP-binding cassette domain II of the excision repair protein UvrA. Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
97COG11012637597.90.00038[                                 -------------   ]PhnKABC-type uncharacterized transport system, ATPase component
98TIGR044355557297.90.00014[                                 ------------    ]restrict_AAA_1restriction system-associated AAA family ATPase. Members of this family are AAA family ATPases by homology. They occur regularly in a conserved gene neighborhood with the restriction (R), modification (M), and specificity (S) proteins of an apparent type I restriction enzyme system, plus one additional uncharacterized protein. It is not clear whether members of this family contribute to restriction per se, or to another process such as transfer of mobile elements.
99PRK142402507397.90.00021[                                  ------------   ]PRK14240phosphate transporter ATP-binding protein; Provisional
100cd032772134297.81.6E-05[------                                           ]ABC_SMC5_eukATP-binding cassette domain of eukaryotic SMC5 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
101PRK022248804597.81.3E-05[------                                           ]PRK02224chromosome segregation protein; Provisional
102TIGR038642367497.80.00014[                                 -------------   ]PQQ_ABC_ATPABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system. Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification.
103COG11253097697.80.0002[                                 -------------   ]OpuBAABC-type proline/glycine betaine transport system, ATPase component
104PRK142362725797.82.2E-05[                                  ---------      ]PRK14236phosphate transporter ATP-binding protein; Provisional
105COG04885307897.80.00026[                                 -------------   ]UupATPase components of ABC transporters with duplicated ATPase domains
106TIGR011883027597.89.7E-05[                                 -------------   ]drrAdaunorubicin resistance ABC transporter ATP-binding subunit. This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc.
107COG11192577497.80.00016[                                 -------------   ]ModFABC-type molybdenum transport system, ATPase component/photorepair protein PhrA
108PRK036952485497.88.7E-05[                                      --------   ]PRK03695vitamin B12-transporter ATPase; Provisional
109cd032281716897.80.00022[                                  -----------    ]ABCC_MRP_LikeATP-binding cassette domain of multidrug resistance protein-like transporters. The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
110COG04443167697.80.00032[                                 -------------   ]DppDABC-type dipeptide/oligopeptide/nickel transport system, ATPase component
111cd032202247797.80.00054[                                 -------------   ]ABC_KpsT_WztATP-binding cassette component of polysaccharide transport system. The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
112cd032271626097.82.6E-05[                                  ---------      ]ABC_Class2ATP-binding cassette domain of non-transporter proteins. ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
113PRK142532495697.80.0003[                                  ---------      ]PRK14253phosphate ABC transporter ATP-binding protein; Provisional
114PRK142422535697.70.00034[                                  ---------      ]PRK14242phosphate transporter ATP-binding protein; Provisional
115PRK142372675797.70.00019[                                  ---------      ]PRK14237phosphate transporter ATP-binding protein; Provisional
116PRK142622505897.70.00011[                                  ---------      ]PRK14262phosphate ABC transporter ATP-binding protein; Provisional
117COG46742497097.70.00016[                                  -----------    ]COG4674ABC-type uncharacterized transport system, ATPase component
118cd032792134597.74.1E-05[------                                           ]ABC_sbcCDATP-binding cassette domain of sbcCD. SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
119COG11342497797.70.00095[                                 -------------   ]TagHABC-type polysaccharide/polyol phosphate transport system, ATPase component
120cd032952427697.70.00041[                                 -------------   ]ABC_OpuCA_OsmoprotectionATP-binding cassette domain of the osmoprotectant transporter. OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
121cd032412766597.70.00097[----------                                       ]ABC_RecNATP-binding cassette domain of RecN. RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
122TIGR030052528297.70.00037[                                  -------------- ]ectoine_ehuAectoine/hydroxyectoine ABC transporter, ATP-binding protein. Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
123COG22747097297.70.00023[                                  ------------   ]SunTABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain
124COG41523006097.70.00029[                                 ----------      ]YhaQABC-type uncharacterized transport system, ATPase component
125PRK142482687497.70.00033[                                  ------------   ]PRK14248phosphate ABC transporter ATP-binding protein; Provisional
126PRK142432645797.70.00028[                                  ---------      ]PRK14243phosphate transporter ATP-binding protein; Provisional
127COG11325677397.70.00053[                                  ------------   ]MdlBABC-type multidrug transport system, ATPase and permease component
128COG41332096097.70.00022[                                 ----------      ]CcmAABC-type transport system involved in cytochrome c biogenesis, ATPase component
129PRK095364027497.70.00019[                                 -------------   ]btuDcorrinoid ABC transporter ATPase; Reviewed
130COG38393387797.60.0004[                                 -------------   ]MalKABC-type sugar transport system, ATPase component
131cd032652207597.60.00026[                                 -------------   ]ABC_DrrADaunorubicin/doxorubicin resistance ATP-binding protein. DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
132cd032732514697.62.8E-05[------                                           ]ABC_SMC2_eukATP-binding cassette domain of eukaryotic SMC2 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
133PRK1407934927097.60.00044[------------------------------------------       ]recFrecombination protein F; Provisional
134COG04885307197.60.00084[                                 ------------    ]UupATPase components of ABC transporters with duplicated ATPase domains
135cd032172005597.60.00041[                                      --------   ]ABC_FeS_AssemblyABC-type transport system involved in Fe-S cluster assembly, ATPase component. Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
136PRK142632615697.60.00043[                                  ---------      ]PRK14263phosphate ABC transporter ATP-binding protein; Provisional
137TIGR034102307497.60.00095[                                  ------------   ]urea_trans_UrtEurea ABC transporter, ATP-binding protein UrtE. Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity.
138COG11235397697.60.0011[                                 -------------   ]GsiAABC-type glutathione transport system ATPase component, contains duplicated ATPase domain
139PRK142352675797.50.00025[                                  ---------      ]PRK14235phosphate transporter ATP-binding protein; Provisional
140cd032972147497.50.0018[                                 -------------   ]ABC_ModC_molybdenum_transporterATP-binding cassette domain of the molybdenum transport system. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
141PRK142672535797.50.00053[                                  ---------      ]PRK14267phosphate ABC transporter ATP-binding protein; Provisional
142cd032582337597.50.0012[                                 -------------   ]ABC_MetN_methionine_transporterATP-binding cassette domain of methionine transporter. MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
143TIGR012883035997.50.00027[                                 ----------      ]nodIATP-binding ABC transporter family nodulation protein NodI. This protein is required for normal nodulation by nitrogen-fixing root nodule bacteria such as Mesorhizobium loti. It is a member of the family of ABC transporter ATP binding proteins and works with NodJ to export a nodulation signal molecule. This model does not recognize the highly divergent NodI from Azorhizobium caulinodans.
144PRK142452505697.40.0021[                                  ---------      ]PRK14245phosphate ABC transporter ATP-binding protein; Provisional
145PRK142612535797.40.00033[                                  ---------      ]PRK14261phosphate ABC transporter ATP-binding protein; Provisional
146PRK142742595697.40.00057[                                  ---------      ]PRK14274phosphate ABC transporter ATP-binding protein; Provisional
147cd032922147097.40.0021[                                  -----------    ]ABC_FtsE_transporterATP-binding cassette domain of the cell division transporter. FtsE is a hydrophilic nucleotide-binding protein that binds FtsX to form a heterodimeric ATP-binding cassette (ABC)-type transporter that associates with the bacterial inner membrane. The FtsE/X transporter is thought to be involved in cell division and is important for assembly or stability of the septal ring.
148PRK135363405997.40.00033[                                 ----------      ]PRK13536nodulation factor exporter subunit NodI; Provisional
149PRK136492808897.40.00089[                                  ---------------]cbiOcobalt transporter ATP-binding subunit; Provisional
150COG49875737297.40.0021[                                  ------------   ]CydCABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components
151COG38423527897.40.00078[                                 -------------   ]PotAABC-type Fe3+/spermidine/putrescine transport systems, ATPase components
152PRK111533437497.40.0024[                                  ------------   ]metNDL-methionine transporter ATP-binding subunit; Provisional
153PRK142702515697.40.00016[                                  ---------      ]PRK14270phosphate ABC transporter ATP-binding protein; Provisional
154TIGR019782437397.40.0035[                                  ------------   ]sufCFeS assembly ATPase SufC. SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA.
155PRK136372878897.30.00035[                                  ---------------]cbiOcobalt transporter ATP-binding subunit; Provisional
156TIGR037402235897.30.00063[                                 ----------      ]galliderm_ABCgallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit. Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
157TIGR012772137597.30.0043[                                  ------------   ]thiQthiamine ABC transporter, ATP-binding protein. This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found.
158COG11235397697.30.0044[                                 -------------   ]GsiAABC-type glutathione transport system ATPase component, contains duplicated ATPase domain
159cd032542297397.30.0084[                                  ------------   ]ABCC_Glucan_exporter_likeATP-binding cassette domain of glucan transporter and related proteins, subfamily C. Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
160COG46192237797.30.0035[                                 -------------   ]FetAABC-type iron transport system FetAB, ATPase component
161pfam000051502697.30.00024[  ----                                           ]ABC_tranABC transporter. ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
162TIGR037712236897.30.00069[                                 ------------    ]anch_rpt_ABCanchored repeat-type ABC transporter, ATP-binding subunit. This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown.
163COG11295007597.30.0043[                                 -------------   ]MglAABC-type sugar transport system, ATPase component
164cd032942697797.20.0052[                                 -------------   ]ABC_Pro_Gly_BetaineATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system. This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
165COG38402317697.20.0073[                                 -------------   ]ThiQABC-type thiamine transport system, ATPase component
166TIGR026732147097.20.0015[                                  -----------    ]FtsEcell division ATP-binding protein FtsE. This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein.
167PRK142522655597.20.0017[                                  ---------      ]PRK14252phosphate ABC transporter ATP-binding protein; Provisional
168PRK136313207297.20.0004[                                  ------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
169PRK107442605797.20.00084[                                  ---------      ]pstBphosphate transporter ATP-binding protein; Provisional
170TIGR0061810424497.20.00038[------                                           ]sbccexonuclease SbcC. All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
171cd002671576997.20.00029[                                  -----------    ]ABC_ATPaseATP-binding cassette transporter nucleotide-binding domain. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
172TIGR037195526997.10.0044[                                -----------      ]ABC_ABC_ChvDATP-binding cassette protein, ChvD family. Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
173PRK117012587597.10.0019[                                  ------------   ]phnKphosphonate C-P lyase system protein PhnK; Provisional
174TIGR009587117397.10.004[                                  ------------   ]3a01208Conjugate Transporter-2 (CT2) Family protein.
175PRK135373067297.10.0033[                                 ------------    ]PRK13537nodulation ABC transporter NodI; Provisional
176COG46185807197.10.0062[                                  ------------   ]ArpDABC-type protease/lipase transport system, ATPase and permease components
177PRK142752867397.00.0031[                                  ------------   ]PRK14275phosphate ABC transporter ATP-binding protein; Provisional
178cd032982117597.00.011[                                 -------------   ]ABC_ThiQ_thiamine_transporterATP-binding cassette domain of the thiamine transport system. Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
179PRK142682585597.00.0013[                                  ---------      ]PRK14268phosphate ABC transporter ATP-binding protein; Provisional
180COG11372437297.00.011[                                  ------------   ]LptBABC-type lipopolysaccharide export system, ATPase component
181PRK118195566997.00.0085[                                -----------      ]PRK11819putative ABC transporter ATP-binding protein; Reviewed
182PRK113002557197.00.0011[                                  -----------    ]livGleucine/isoleucine/valine transporter ATP-binding subunit; Provisional
183COG41753867697.00.011[                                 -------------   ]ProVABC-type proline/glycine betaine transport system, ATPase component
184cd032182327296.90.011[                                  ------------   ]ABC_YhbGATP-binding cassette component of YhbG transport system. The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
185PRK142412585796.90.0078[                                  ---------      ]PRK14241phosphate transporter ATP-binding protein; Provisional
186COG45592598296.90.00061[                                 -------------   ]COG4559ABC-type hemin transport system, ATPase component
187PRK142462577396.90.01[                                 -------------   ]PRK14246phosphate ABC transporter ATP-binding protein; Provisional
188COG41725347696.90.013[                                 -------------   ]YejFABC-type microcin C transport system, duplicated ATPase component YejF
189TIGR028575295796.90.008[                                  ---------      ]CydDthiol reductant ABC exporter, CydD subunit. The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
190TIGR034153828396.90.0077[                               ---------------   ]ABC_choXWV_ATPcholine ABC transporter, ATP-binding protein. Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines.
191cd032992357696.90.02[                                 -------------   ]ABC_ModC_likeATP-binding cassette domain similar to the molybdate transporter. Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
192PRK142582614696.90.013[                                  -------        ]PRK14258phosphate ABC transporter ATP-binding protein; Provisional
193cd033012137696.80.016[                                 -------------   ]ABC_MalK_NThe N-terminal ATPase domain of the maltose transporter, MalK. ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
194COG11162486996.80.016[                                  -----------    ]TauBABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component
195cd032211446696.80.00092[                                  -----------    ]ABCF_EF-3ATP-binding cassette domain of elongation factor 3, subfamily F. Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
196PRK142573295696.80.025[                                  ---------      ]PRK14257phosphate ABC transporter ATP-binding protein; Provisional
197PRK111476357696.80.0083[                                 -------------   ]PRK11147ABC transporter ATPase component; Reviewed
198TIGR0060613114096.70.00087[------                                           ]rad50rad50. All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
199TIGR011863637596.70.03[                                  ------------   ]proVglycine betaine/L-proline transport ATP binding subunit. This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature.
200PRK112885019596.70.074[                                 ----------------]araGL-arabinose transporter ATP-binding protein; Provisional
201PRK134095907796.70.023[                                 -------------   ]PRK13409putative ATPase RIL; Provisional
202PRK011568954496.70.0015[------                                           ]PRK01156chromosome segregation protein; Provisional
203COG38455017496.60.02[                                 -------------   ]YufOABC-type uncharacterized transport system, ATPase component
204cd032532367196.60.015[                                  ------------   ]ABCC_ATM1_transporterATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C. ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
205PRK111605748296.60.024[                                  -------------- ]PRK11160cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
206TIGR006309256696.60.0048[                                 ----------      ]uvraexcinuclease ABC, A subunit. This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
207cd002671572696.60.012[  ----                                           ]ABC_ATPaseATP-binding cassette transporter nucleotide-binding domain. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
208PRK142492516696.60.0066[                                  -----------    ]PRK14249phosphate ABC transporter ATP-binding protein; Provisional
209TIGR021423547496.50.014[                                 -------------   ]modC_ABCmolybdenum ABC transporter, ATP-binding protein. This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter.
210TIGR028685304596.50.0095[                                  -------        ]CydCthiol reductant ABC exporter, CydC subunit. The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
211COG41725347596.50.0088[                                 -------------   ]YejFABC-type microcin C transport system, duplicated ATPase component YejF
212cd032362557796.50.043[                                 -------------   ]ABC_RNaseL_inhibitor_domain1The ATP-binding cassette domain 1 of RNase L inhibitor. The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
213cd032932207596.50.033[                                 -------------   ]ABC_NrtD_SsuB_transportersATP-binding cassette domain of the nitrate and sulfonate transporters. NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
214PRK142382717196.40.0059[                                  ------------   ]PRK14238phosphate transporter ATP-binding protein; Provisional
215COG12455917596.40.041[                                 ------------    ]Rli1Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains
216PRK142662505696.40.0045[                                  ---------      ]PRK14266phosphate ABC transporter ATP-binding protein; Provisional
217TIGR0095613944996.40.01[                                      -------    ]3a01205Pleiotropic Drug Resistance (PDR) Family protein.
218PRK142652745696.30.0085[                                  ---------      ]PRK14265phosphate ABC transporter ATP-binding protein; Provisional
219cd032442217496.30.094[                                  ------------   ]ABCC_MRP_domain2ATP-binding cassette domain 2 of multidrug resistance-associated protein. The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
220cd032312015896.30.0028[                                 ----------      ]ABC_CcmA_heme_exporterCytochrome c biogenesis ATP-binding export protein. CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
221PRK136432885396.30.011[                                      --------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
222PRK142512516096.30.0042[                                 ----------      ]PRK14251phosphate ABC transporter ATP-binding protein; Provisional
223TIGR029822205796.20.03[                                  ---------      ]heterocyst_DevAABC exporter ATP-binding subunit, DevA family. Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
224COG01789356696.20.0065[                                 ----------      ]UvrAExcinuclease UvrABC ATPase subunit
225COG04975574396.20.0055[------                                           ]RecNDNA repair ATPase RecN
226COG41483528596.20.021[                                  -------------- ]ModCABC-type molybdate transport system, ATPase component
227PRK104192687796.20.13[                                 -------------   ]nikEnickel transporter ATP-binding protein NikE; Provisional
228cd032892757496.20.031[                                  ------------   ]ABCC_CFTR2ATP-binding cassette domain 2 of CFTR,subfamily C. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
229TIGR023242245196.10.0068[                                 ---------       ]CP_lyasePhnLphosphonate C-P lyase system protein PhnL. Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
230TIGR0127114905796.10.022[                                  ---------      ]CFTR_proteincystic fibrosis transmembrane conductor regulator (CFTR). The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se.
231TIGR018425445696.10.031[                                  ---------      ]type_I_sec_PrtDtype I secretion system ABC transporter, PrtD family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion.
232PRK142722526196.00.017[                                 ----------      ]PRK14272phosphate ABC transporter ATP-binding protein; Provisional
233TIGR037976867396.00.066[                                  ------------   ]NHLM_micro_ABC2NHLM bacteriocin system ABC transporter, ATP-binding protein. Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes.
234PRK003499436296.00.028[                                 ----------      ]uvrAexcinuclease ABC subunit A; Reviewed
235PRK136342907296.00.029[                                  ------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
236COG41382483596.00.0041[                                      -----      ]BtuDABC-type cobalamin transport system, ATPase component
237PRK107712327496.00.14[                                  ------------   ]thiQthiamine transporter ATP-binding subunit; Provisional
238cd000091512596.00.0066[  ----                                           ]AAAThe AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
239PRK142562525795.90.006[                                  ---------      ]PRK14256phosphate ABC transporter ATP-binding protein; Provisional
240PRK111745887295.90.16[                                  ------------   ]PRK11174cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
241PRK142712769295.90.019[                                  ---------------]PRK14271phosphate ABC transporter ATP-binding protein; Provisional
242TIGR011891985895.90.0059[                                 ----------      ]ccmAheme ABC exporter, ATP-binding protein CcmA. This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c.
243cd032761984295.80.011[------                                           ]ABC_SMC6_eukATP-binding cassette domain of eukaryotic SM6 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
244PRK134095905995.80.046[                                 ----------      ]PRK13409putative ATPase RIL; Provisional
245cd032161637295.80.0074[                                  ------------   ]ABC_Carb_Monos_IFirst domain of the ATP-binding cassette component of monosaccharide transport system. This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
246PRK142602595695.80.012[                                  ---------      ]PRK14260phosphate ABC transporter ATP-binding protein; Provisional
247cd032342265095.70.14[                                 ---------       ]ABCG_WhiteWhite pigment protein homolog of ABCG transporter subfamily. The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
248PRK142502417795.70.069[                                 -------------   ]PRK14250phosphate ABC transporter ATP-binding protein; Provisional
249cd032432022695.70.0091[  ----                                           ]ABC_MutS_homologsATP-binding cassette domain of MutS homologs. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
250PRK136322717395.70.059[                                 -------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
251cd032862182495.60.011[  ----                                           ]ABC_MSH6_eukATP-binding cassette domain of eukaryotic MutS6 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
252pfam132071142395.60.012[  ----                                           ]AAA_17AAA domain.
253COG47179847895.60.019[------------                                     ]YhaNUncharacterized protein YhaN, contains AAA domain
254PRK150562727995.60.016[                                 -------------   ]PRK15056manganese/iron transporter ATP-binding protein; Provisional
255PRK142552527395.60.012[                                  ------------   ]PRK14255phosphate ABC transporter ATP-binding protein; Provisional
256cd032482265095.50.011[                                  --------       ]ABCC_TAPATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C. TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
257COG41672677695.50.1[                                 -------------   ]SapFABC-type antimicrobial peptide transport system, ATPase component
258PRK142392527395.50.01[                                  ------------   ]PRK14239phosphate transporter ATP-binding protein; Provisional
259PRK106366385995.50.024[                                 ----------      ]PRK10636putative ABC transporter ATP-binding protein; Provisional
260cd032372465995.50.011[                                 ----------      ]ABC_RNaseL_inhibitor_domain2The ATP-binding cassette domain 2 of RNase L inhibitor. The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
261pfam004882352495.40.02[  ----                                           ]MutS_VMutS domain V. This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.
262cd033002327695.40.11[                                 -------------   ]ABC_PotA_NATP-binding cassette domain of the polyamine transporter. PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
263TIGR032653537495.40.41[                                  ------------   ]PhnT2putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein. This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely.
264PRK111443528595.40.099[                                  -------------- ]modCmolybdate transporter ATP-binding protein; Provisional
265PRK102532655095.40.014[                                 ---------       ]PRK10253iron-enterobactin transporter ATP-binding protein; Provisional
266PRK135495067595.30.24[                                 -------------   ]PRK13549xylose transporter ATP-binding subunit; Provisional
267TIGR027692657795.30.25[                                 -------------   ]nickel_nikEnickel import ATP-binding protein NikE. This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase.
268PRK111476352695.30.011[  ----                                           ]PRK11147ABC transporter ATPase component; Reviewed
269PRK142692464895.30.087[                                  --------       ]PRK14269phosphate ABC transporter ATP-binding protein; Provisional
270TIGR031856504595.30.011[------                                           ]DNA_S_dndDDNA sulfur modification protein DndD. This model describes the DndB protein encoded by an operon associated with a sulfur-containing modification to DNA. The operon is sporadically distributed in bacteria, much like some restriction enzyme operons. DndD is described as a putative ATPase. The small number of examples known so far include species from among the Firmicutes, Actinomycetes, Proteobacteria, and Cyanobacteria.
271pfam000041312295.30.014[   ---                                           ]AAAATPase family associated with various cellular activities (AAA). AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
272cd032962397995.10.019[                                 -------------   ]ABC_CysA_sulfate_importerATP-binding cassette domain of the sulfate transporter. Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
273PRK136502798495.10.008[                                 --------------- ]cbiOcobalt transporter ATP-binding subunit; Provisional
274COG47782353595.10.028[-----                                            ]PhnLAlpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
275cd032492387395.00.62[                                  ------------   ]ABC_MTABC3_MDL1_MDL2ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins. MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
276TIGR009682377695.00.018[                                  ------------   ]3a0106s01sulfate ABC transporter, ATP-binding protein.
277PRK105225476795.00.11[                                -----------      ]PRK10522multidrug transporter membrane component/ATP-binding component; Provisional
278TIGR006345634395.00.0095[------                                           ]recNDNA repair protein RecN. All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair.
279PRK150645305895.00.12[                                 ----------      ]PRK15064ABC transporter ATP-binding protein; Provisional
280cd032842162495.00.022[  ----                                           ]ABC_MutS1ATP-binding cassette domain of MutS1 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
281TIGR023143437294.90.27[                                  ------------   ]ABC_MetND-methionine ABC transporter, ATP-binding protein. Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
282PRK136522775394.90.043[                                      --------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
283PRK136402829194.90.037[                                 ----------------]cbiOcobalt transporter ATP-binding subunit; Provisional
284COG46155466894.80.23[                                -----------      ]PvdEABC-type siderophore export system, fused ATPase and permease components
285pfam131667137194.80.021[                                 ----------      ]AAA_13AAA domain. This family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
286PRK099842626794.60.05[                                 -----------     ]PRK09984phosphonate/organophosphate ester transporter subunit; Provisional
287COG12455915194.50.27[                                 ---------       ]Rli1Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains
288cd032221772294.40.026[  ---                                            ]ABC_RNaseL_inhibitorATP-binding cassette domain of RNase L inhibitor. The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
289PRK142592695794.40.042[                                  ---------      ]PRK14259phosphate ABC transporter ATP-binding protein; Provisional
290TIGR022045769094.30.6[                                  ---------------]MsbA_relABC transporter, permease/ATP-binding protein. This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
291PRK053998542494.30.049[  ----                                           ]PRK05399DNA mismatch repair protein MutS; Provisional
292cd032822042494.20.039[  ----                                           ]ABC_MSH4_eukATP-binding cassette domain of eukaryotic MutS4 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
293PRK135382046194.20.049[                                 ----------      ]PRK13538cytochrome c biogenesis protein CcmA; Provisional
294COG02498432494.20.042[  ----                                           ]MutSDNA mismatch repair ATPase MutS
295PRK116503564094.10.041[                                 -------         ]ugpCglycerol-3-phosphate transporter ATP-binding subunit; Provisional
296PRK110003692394.10.041[  ----                                           ]PRK11000maltose/maltodextrin transporter ATP-binding protein; Provisional
297cd032231664994.10.039[                                  --------       ]ABCD_peroxisomal_ALDPATP-binding cassette domain of peroxisomal transporter, subfamily D. Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
298cd032131947194.10.048[                                  -----------    ]ABCG_EPDREye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily. ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
299cd032461735693.90.06[                                  ---------      ]ABCC_Protease_SecretionATP-binding cassette domain of PrtD, subfamily C. This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
300TIGR011873257693.90.2[                                 -------------   ]potAspermidine/putrescine ABC transporter ATP-binding subunit. This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included).
301TIGR009556177293.90.8[                                  ------------   ]3a01204The Eye Pigment Precursor Transporter (EPP) Family protein.
302PRK136462867293.90.05[                                  ------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
303cd032502046893.80.061[                                  -----------    ]ABCC_MRP_domain1ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C. This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
304COG28053532693.80.069[  ----                                           ]PilTTfp pilus assembly protein PilT, pilus retraction ATPase
305pfam131911562693.60.081[  ----                                           ]AAA_16AAA ATPase domain. This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.
306cd032161632693.50.5[  ----                                           ]ABC_Carb_Monos_IFirst domain of the ATP-binding cassette component of monosaccharide transport system. This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
307TIGR027702307393.40.19[                                  ------------   ]nickel_nikDnickel import ATP-binding protein NikD. This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous.
308PRK118195565893.30.058[                                 ----------      ]PRK11819putative ABC transporter ATP-binding protein; Reviewed
309PRK1024610474493.30.062[------                                           ]PRK10246exonuclease subunit SbcC; Provisional
310PRK150645305193.30.081[                                     --------    ]PRK15064ABC transporter ATP-binding protein; Provisional
311cd011311982193.20.066[  ---                                            ]PilTPilus retraction ATPase PilT. PilT is a nucleotide binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.
312PRK135472723293.10.068[                                     -----       ]hmuVhemin importer ATP-binding subunit; Provisional
313PRK136412875493.10.94[                                     ---------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
314PRK102472252893.10.041[  ----                                           ]PRK10247putative ABC transporter ATP-binding protein YbbL; Provisional
315pfam135211622293.00.079[  ----                                           ]AAA_28AAA domain.
316TIGR037195525892.90.072[                                 ----------      ]ABC_ABC_ChvDATP-binding cassette protein, ChvD family. Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
317cd032211442392.80.42[  ----                                           ]ABCF_EF-3ATP-binding cassette domain of elongation factor 3, subfamily F. Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
318cd000711374892.80.084[  --------                                       ]GMPKGuanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
319PRK092702292792.70.11[  ----                                           ]PRK09270nucleoside triphosphate hydrolase domain-containing protein; Reviewed
320PRK105752652992.60.09[                                      ----       ]PRK10575iron-hydroxamate transporter ATP-binding subunit; Provisional
321pfam136711432192.60.092[  ---                                            ]AAA_33AAA domain. This family of domains contain only a P-loop motif, that is characteristic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
322PRK095442512792.60.024[  ----                                           ]znuChigh-affinity zinc transporter ATPase; Reviewed
323cd032702266192.50.088[                                 ----------      ]ABC_UvrA_IATP-binding cassette domain I of the excision repair protein UvrA. Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
324PRK136352797492.40.093[                                 -------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
325cd032512347392.30.13[                                  ------------   ]ABCC_MsbAATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C. MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
326PRK081181672592.20.13[  ----                                           ]PRK08118topology modulation protein; Reviewed
327PRK109384901692.20.034[   --                                            ]PRK10938putative molybdenum transport ATP-binding protein ModF; Provisional
328COG05631782292.10.13[  ----                                           ]AdkAdenylate kinase or related kinase
329PRK149743362692.10.13[  ----                                           ]PRK14974cell division protein FtsY; Provisional
330PRK136522772791.90.11[  ----                                           ]cbiOcobalt transporter ATP-binding subunit; Provisional
331PRK0486314864191.90.13[------                                           ]mukBcell division protein MukB; Provisional
332PRK109824917591.90.68[                                 -------------   ]PRK10982galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
333cd032812132791.90.13[  ----                                           ]ABC_MSH5_eukATP-binding cassette domain of eukaryotic MutS5 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
334cd032831992491.70.15[  ----                                           ]ABC_MutS-likeATP-binding cassette domain of MutS-like homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
335pfam057291652591.70.19[  ----                                           ]NACHTNACHT domain. This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.
336TIGR044062393091.60.099[----                                             ]LPS_export_lptBLPS export ABC transporter ATP-binding protein. Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export.
337COG31721872791.60.078[  ----                                           ]NadR3Nicotinamide riboside kinase
338COG01941914791.50.16[  --------                                       ]GmkGuanylate kinase
339pfam004481952691.50.2[  ----                                           ]SRP54SRP54-type protein, GTPase domain. This family includes relatives of the G-domain of the SRP54 family of proteins.
340cd032852222391.50.14[  ----                                           ]ABC_MSH2_eukATP-binding cassette domain of eukaryotic MutS2 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
341PRK097005107591.40.85[                                  ------------   ]PRK09700D-allose transporter ATP-binding protein; Provisional
342TIGR014203432491.40.14[  ----                                           ]pilT_fampilus retraction protein PilT. This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation.
343cd032131942491.40.26[  ----                                           ]ABCG_EPDREye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily. ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
344pfam134011242491.30.2[  ----                                           ]AAA_22AAA domain.
345PRK095802485591.30.092[                                     ---------   ]sufCcysteine desulfurase ATPase component; Reviewed
346COG41812287191.30.16[                                  ------------   ]YbbAPredicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component
347COG46082687691.20.75[                                 -------------   ]AppFABC-type oligopeptide transport system, ATPase component
348cd041702682691.20.14[   ---                                           ]EF-G_bactElongation factor G (EF-G) family. Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
349cd032872222691.10.16[  ----                                           ]ABC_MSH3_eukATP-binding cassette domain of eukaryotic MutS3 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
350pfam031931612491.10.17[  ----                                           ]DUF258Protein of unknown function, DUF258.
351pfam13245722590.80.31[  ----                                           ]AAA_19Part of AAA domain.
352cd020211502690.70.21[  ----                                           ]GntKGluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
353PRK136382717490.60.13[                                 -------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
354PRK138308182690.60.25[  ----                                           ]PRK13830conjugal transfer protein TrbE; Provisional
355PRK0063518097790.50.38[                             -------------       ]PRK00635excinuclease ABC subunit A; Provisional
356TIGR032631794790.50.24[  --------                                       ]guanyl_kinguanylate kinase. Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP.
357COG12224062390.40.19[  ----                                           ]RPT1ATP-dependent 26S proteasome regulatory subunit
358cd032321922990.30.23[                                      ----       ]ABCG_PDR_domain2Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters. The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
359cd018822312790.30.23[  ----                                           ]BMS1Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes. Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
360pfam009101052390.20.29[   ---                                           ]RNA_helicaseRNA helicase. This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.
361PRK114323514890.20.8[                                  --------       ]fbpCferric transporter ATP-binding subunit; Provisional
362cd033692077590.10.33[                                  ------------   ]ABCC_NFT1ATP-binding cassette domain 2 of NFT1, subfamily C. Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
363PRK151122677490.10.2[                                 -------------   ]PRK15112antimicrobial peptide ABC system ATP-binding protein SapF; Provisional
364cd032522378089.84.9[                                  -------------- ]ABCC_HemolysinATP-binding cassette domain of hemolysin B, subfamily C. The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
365cd032381765589.80.41[--------                                         ]ABC_UvrAATP-binding cassette domain of the excision repair protein UvrA. Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
366cd02019692289.80.37[   ---                                           ]NKNucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
367TIGR022112217389.70.34[                                 -------------   ]LolD_lipo_exlipoprotein releasing system, ATP-binding protein. This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina.
368PRK041954822789.70.25[  ----                                           ]PRK04195replication factor C large subunit; Provisional
369PRK039923892389.70.22[  ----                                           ]PRK03992proteasome-activating nucleotidase; Provisional
370cd004641542589.70.31[   ---                                           ]SKShikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
371pfam132381282489.60.28[   ---                                           ]AAA_18AAA domain.
372PRK136482695889.60.24[                                 ----------      ]cbiOcobalt transporter ATP-binding subunit; Provisional
373cd018542112289.50.26[  ---                                            ]YjeQ_EngCRibosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases. YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
374cd032471787389.40.34[                                  ------------   ]ABCC_cytochrome_bdATP-binding cassette domain of CydCD, subfamily C. The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
375pfam077281352389.40.35[   ---                                           ]AAA_5AAA domain (dynein-related subfamily). This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
376pfam032051382689.20.43[  ----                                           ]MobBMolybdopterin guanine dinucleotide synthesis protein B. This protein contains a P-loop.
377pfam131731272289.20.39[  ---                                            ]AAA_14AAA domain. This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.
378pfam016372232589.10.37[  ----                                           ]Arch_ATPaseArchaeal ATPase. This family contain a conserved P-loop motif that is involved in binding ATP. This family is almost exclusively found in archaebacteria and particularly in Methanococcus jannaschii that encodes sixteen members of this family.
379COG41851872588.90.1[  ----                                           ]COG4185Predicted ABC-type ATPase
380PRK142732545688.90.43[                                  ---------      ]PRK14273phosphate ABC transporter ATP-binding protein; Provisional
381COG28045002688.80.38[  ----                                           ]PulEType II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB
382COG50083752088.70.42[  ---                                            ]PilUTfp pilus assembly protein, ATPase PilU
383COG46391681988.50.31[  ---                                            ]COG4639Predicted kinase
384COG45252596788.30.41[                                  -----------    ]TauBABC-type taurine transport system, ATPase component
385COG07031722688.30.4[  ----                                           ]AroKShikimate kinase
386COG42403002688.20.46[  ----                                           ]Tda10Pantothenate kinase-related protein Tda10 (topoisomerase I damage affected protein)
387PRK003002054488.20.44[  --------                                       ]gmkguanylate kinase; Provisional
388PRK136332807388.10.26[                                 -------------   ]PRK13633cobalt transporter ATP-binding subunit; Provisional
389TIGR036082062988.10.47[ -----                                           ]L_ocin_972_ABCputative bacteriocin export ABC transporter, lactococcin 972 group. A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins.
390COG24015935988.01.1[                                 ----------      ]MK0520ABC-type ATPase fused to a predicted acetyltransferase domain
391PRK150793317587.93.9[                                 -------------   ]PRK15079oligopeptide ABC transporter ATP-binding protein OppF; Provisional
392PRK133424132687.90.42[  ----                                           ]PRK13342recombination factor protein RarA; Reviewed
393COG05523402687.80.46[  ----                                           ]FtsYSignal recognition particle GTPase
394cd041641592187.80.48[  ---                                            ]trmEtrmE is a tRNA modification GTPase. TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
395TIGR004551842787.80.47[  ----                                           ]apsKadenylyl-sulfate kinase. This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment.
396PRK108513537787.70.36[                                 -------------   ]PRK10851sulfate/thiosulfate transporter subunit; Provisional
397PRK113083275887.76.8[                                 ----------      ]dppFdipeptide transporter ATP-binding subunit; Provisional
398TIGR025334862687.70.37[  ----                                           ]type_II_gspEtype II secretion system protein E. This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis.
399PRK135432144787.60.58[                                 --------        ]PRK13543cytochrome c biogenesis protein CcmA; Provisional
400PRK053424122787.30.49[  ----                                           ]clpXATP-dependent protease ATP-binding subunit ClpX; Provisional
401cd011292642687.20.4[  ----                                           ]PulE-GspEPulE/GspE The type II secretory pathway is the main terminal branch of the general secretory pathway (GSP). It is responsible for the export the majority of Gram-negative bacterial exoenzymes and toxins. PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PillB and HofB.
402pfam019261141987.10.54[   --                                            ]MMR_HSR150S ribosome-binding GTPase. The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
403COG41072587587.00.62[                                  ------------   ]PhnKABC-type phosphonate transport system, ATPase component
404COG22564362686.60.51[  ----                                           ]RarAReplication-associated recombination protein RarA (DNA-dependent ATPase)
405PRK000982982786.60.5[  ----                                           ]PRK00098GTPase RsgA; Reviewed
406PRK122893522486.60.51[  ----                                           ]PRK12289GTPase RsgA; Reviewed
407PRK067621662686.60.72[  ----                                           ]PRK06762hypothetical protein; Provisional
408COG41072582686.52.5[  ----                                           ]PhnKABC-type phosphonate transport system, ATPase component
409PRK001311752786.50.57[  ----                                           ]aroKshikimate kinase; Reviewed
410TIGR009546595786.40.53[                                  ---------      ]3a01203Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein.
411COG41786044686.30.52[                                  -------        ]YddAABC-type uncharacterized transport system, permease and ATPase components
412PRK135411952786.20.39[  ----                                           ]PRK13541cytochrome c biogenesis protein CcmA; Provisional
413pfam024563702186.20.58[  ---                                            ]Adeno_IVa2Adenovirus IVa2 protein. IVa2 protein can interact with the adenoviral packaging signal and that this interaction involves DNA sequences that have previously been demonstrated to be required for packaging. During the course of lytic infection, the adenovirus major late promoter (MLP) is induced to high levels after replication of viral DNA has started. IVa2 is a transcriptional activator of the major late promoter.
414TIGR018466948786.15.7[                                  ---------------]type_I_sec_HlyBtype I secretion system ABC transporter, HlyB family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion.
415PRK136575887386.10.6[                                  ------------   ]PRK13657cyclic beta-1,2-glucan ABC transporter; Provisional
416TIGR025253722586.10.55[  ----                                           ]plasmid_TraJplasmid transfer ATPase TraJ. Members of this protein family are predicted ATPases associated with plasmid transfer loci in bacteria. This family is most similar to the DotB ATPase of a type-IV secretion-like system of obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii (TIGR02524).
417TIGR010708402386.00.61[  ----                                           ]mutS1DNA mismatch repair protein MutS.
418PRK135402002786.00.6[  ----                                           ]PRK13540cytochrome c biogenesis protein CcmA; Provisional
419PRK112482555585.80.66[                                  ---------      ]tauBtaurine transporter ATP-binding subunit; Provisional
420TIGR006309254485.80.45[------                                           ]uvraexcinuclease ABC, A subunit. This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
421TIGR036895122785.60.7[  ----                                           ]pup_AAAproteasome ATPase. In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity.
422COG01789356385.40.42[                                 ----------      ]UvrAExcinuclease UvrABC ATPase subunit
423TIGR015263255285.30.38[  --------                                       ]nadR_NMN_Atransnicotinamide-nucleotide adenylyltransferase, NadR type. The NadR protein of E. coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal to the region covered by this model, is a DNA-binding helix-turn-helix domain (pfam01381) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologs in Mycobacterium tuberculosis, Haemophilus influenzae, and others appear to lack the repressor domain. NadR has recently been shown to act as an enzyme of the salvage pathway of NAD biosynthesis, nicotinamide-nucleotide adenylyltransferase; members of this family are presumed to share this activity. E. coli NadR has also been found to regulate the import of its substrate, nicotinamide ribonucleotide, but it is not known if the other members of this model share that activity.
424cd011201652485.10.74[  ----                                           ]RecA-like_NTPasesRecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H+ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
425PRK107895695785.00.55[                                  ---------      ]PRK10789putative multidrug transporter membrane\ATP-binding components; Provisional
426pfam004372732684.90.77[  ----                                           ]T2SEType II/IV secretion system protein. This family contains both type II and type IV pathway secretion proteins from bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection.
427COG38543082584.80.82[   ---                                           ]SpoIIIAAStage III sporulation protein SpoIIIAA
428COG05291972684.71.1[  ----                                           ]CysCAdenylylsulfate kinase or related kinase
429PRK127275593684.70.63[-----                                            ]PRK12727flagellar biosynthesis regulator FlhF; Provisional
430COG39111832784.60.93[  ----                                           ]COG3911Predicted ATPase
431cd011241872184.50.82[  ---                                            ]KaiCKaiC is a circadian clock protein primarily found in cyanobacteria KaiC is a RecA-like ATPase, having both Walker A and Walker B motifs. A related protein is found in archaea.
432COG12194082784.40.82[  ----                                           ]ClpXATP-dependent protease Clp, ATPase subunit
433cd020201472584.30.91[   ---                                           ]CMPKCytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
434TIGR012423642284.30.75[  ---                                            ]26Sp4526S proteasome subunit P45 family. Many proteins may score above the trusted cutoff because an internal
435TIGR034992822384.20.89[  ----                                           ]FlhFflagellar biosynthetic protein FlhF.
436PRK118312695384.20.94[                                 ---------       ]PRK11831putative ABC transporter ATP-binding protein YrbF; Provisional
437cd008801611984.20.64[   --                                            ]Era_likeE. coli Ras-like protein (Era)-like GTPase. The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
438TIGR023232537484.11.7[                                  ------------   ]CP_lyasePhnKphosphonate C-P lyase system protein PhnK. Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se.
439PRK0063518094584.10.64[------                                           ]PRK00635excinuclease ABC subunit A; Provisional
440TIGR011925857284.11.1[                                  ------------   ]chvAglucan exporter ATP-binding protein. This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related.
441cd011301862684.10.92[  ----                                           ]VirB11-like_ATPaseType IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the Ti (tumor-inducing) plasmid of bacterial to plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11- related ATPases include the archaeal flagella biosynthesis protein and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
442PRK065471722383.80.95[  ----                                           ]PRK06547hypothetical protein; Provisional
443PRK133417252283.60.97[  ---                                            ]PRK13341recombination factor protein RarA/unknown domain fusion protein; Reviewed
444pfam024921782283.61[  ---                                            ]cobWCobW/HypB/UreG, nucleotide-binding domain. This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.
445pfam032661682483.51.2[   ---                                           ]NTPase_1NTPase. This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteristic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.
446TIGR023232532683.41.1[  ----                                           ]CP_lyasePhnKphosphonate C-P lyase system protein PhnK. Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se.
447pfam052721982183.40.93[  ---                                            ]VirEVirulence-associated protein E. This family contains several bacterial virulence-associated protein E like proteins. These proteins contain a P-loop motif.
448cd016722002583.41.3[  ----                                           ]TMPKThymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
449COG519210772583.21.1[  ----                                           ]BMS1GTP-binding protein required for 40S ribosome biogenesis
450TIGR000642772683.10.96[  ----                                           ]ftsYsignal recognition particle-docking protein FtsY. There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein.
451pfam056732482682.91.2[  ----                                           ]DUF815Protein of unknown function (DUF815). This family consists of several bacterial proteins of unknown function.
452COG11002192182.91[  ---                                            ]Gem1GTPase SAR1 family domain
453PRK138738115882.81[                                    ---------    ]PRK13873conjugal transfer ATPase TrbE; Provisional
454PRK116142371982.70.67[  ---                                            ]livFleucine/isoleucine/valine transporter ATP-binding subunit; Provisional
455TIGR022035719082.70.92[                                  ---------------]MsbA_lipidAlipid A export permease/ATP-binding protein MsbA. This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes.
456PRK104182547482.63.1[                                  ------------   ]nikDnickel transporter ATP-binding protein NikD; Provisional
457PRK137682532582.61.3[  ----                                           ]PRK13768GTPase; Provisional
458cd032321922382.31.5[  ----                                           ]ABCG_PDR_domain2Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters. The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
459PRK050571722482.30.96[   ---                                           ]aroKshikimate kinase I; Reviewed
460cd008821612082.20.89[   ---                                           ]Ras_like_GTPaseRat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases). Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
461cd032471782881.86.4[  ----                                           ]ABCC_cytochrome_bdATP-binding cassette domain of CydCD, subfamily C. The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
462COG04703252581.71.2[  ----                                           ]HolBDNA polymerase III, delta prime subunit
463TIGR021731712581.71.1[  ----                                           ]cyt_kin_archcytidylate kinase, putative. Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.
464TIGR012414952181.61.1[  ---                                            ]FtsH_famATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH.
465PRK104163182681.51.4[  ----                                           ]PRK10416signal recognition particle-docking protein FtsY; Provisional
466COG46082682781.31[  ----                                           ]AppFABC-type oligopeptide transport system, ATPase component
467PRK136452897381.21.6[                                  ------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
468PRK124023372781.11.4[  ----                                           ]PRK12402replication factor C small subunit 2; Reviewed
469PRK003499433381.00.86[-----                                            ]uvrAexcinuclease ABC subunit A; Reviewed
470pfam134811922580.91.7[  ----                                           ]AAA_25AAA domain. This AAA domain is found in a wide variety of presumed DNA repair proteins.
471pfam084771182580.91.4[  ----                                           ]MiroMiro-like protein. Mitochondrial Rho proteins (Miro-1 and Miro-2), are atypical Rho GTPases. They have a unique domain organisation, with tandem GTP-binding domains and two EF hand domains (pfam00036), that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.
472COG04672602480.81.5[  ----                                           ]RAD55RecA-superfamily ATPase, KaiC/GvpD/RAD55 family
473PRK108952413080.70.88[----                                             ]PRK10895lipopolysaccharide ABC transporter ATP-binding protein; Provisional
474TIGR039225572780.51.2[  ----                                           ]T7SS_EccAtype VII secretion AAA-ATPase EccA. This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc.
475COG26072873580.40.48[ -----                                           ]COG2607Predicted ATPase, AAA+ superfamily
476cd032332027380.31.5[                                  -----------    ]ABCG_PDR_domain1First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters. The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
477cd020281792680.31.5[  ----                                           ]UMPK_likeUridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).
478cd031161592780.31.9[  ----                                           ]MobBMolybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In E. coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.
479TIGR009297858480.21.4[                                 ------------    ]VirB4_CagEtype IV secretion/conjugal transfer ATPase, VirB4 family. Type IV secretion systems are found in Gram-negative pathogens. They export proteins, DNA, or complexes in different systems and are related to plasmid conjugation systems. This model represents related ATPases that include VirB4 in Agrobacterium tumefaciens (DNA export) CagE in Helicobacter pylori (protein export) and plasmid TraB (conjugation).
480COG40882612780.11.7[  ----                                           ]Kti12tRNA Uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein)
481COG491311044280.11.8[------                                           ]COG4913Uncharacterized protein, contains a C-terminal ATPase domain
482cd018921801780.11.3[   --                                            ]Miro2Mitochondrial Rho family 2 (Miro2), C-terminal. Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.
483TIGR003824132780.11.5[  ----                                           ]clpXendopeptidase Clp ATP-binding regulatory subunit (clpX). A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction.
484COG11623012280.01.3[  ---                                            ]RsgAPutative ribosome biogenesis GTPase RsgA
485PRK108695534479.91.2[------                                           ]PRK10869recombination and repair protein; Provisional
486PRK154395105279.61.2[                                      --------   ]PRK15439autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
487cd020271492479.61.8[   ---                                           ]APSKAdenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
488COG08021492679.31.9[  ----                                           ]TsaEtRNA A37 threonylcarbamoyladenosine biosynthesis protein TsaE
489PRK136422777379.31.1[                                  ------------   ]cbiOcobalt transporter ATP-binding subunit; Provisional
490PRK112472577379.11.7[                                  ------------   ]ssuBaliphatic sulfonates transport ATP-binding subunit; Provisional
491cd041052022179.01.6[  ---                                            ]SR_betaSignal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP). Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.
492TIGR001761552678.91.9[  ----                                           ]mobBmolybdopterin-guanine dinucleotide biosynthesis protein MobB. This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes.
493COG02832222678.42[  ----                                           ]CmkCytidylate kinase
494cd031151732578.22.3[  ----                                           ]SRPThe signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal sighnal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
495pfam003501682078.21.6[   --                                            ]Dynamin_NDynamin family.
496COG22553322678.11.8[  ----                                           ]RuvBHolliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit
497pfam015831572578.12.7[   ---                                           ]APS_kinaseAdenylylsulphate kinase. Enzyme that catalyses the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
498PRK094523751778.01.4[   --                                            ]potAputrescine/spermidine ABC transporter ATPase protein; Reviewed
499TIGR037967107277.91.7[                                  ------------   ]NHLM_micro_ABC1NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein. This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin.
500TIGR032695207477.812[                                  ------------   ]met_CoM_red_A2methyl coenzyme M reductase system, component A2. The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2.