match no.target idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
1TIGR03984147131100.07.2E-31[          -------------------------------------  ]TIGR03984CRISPR-associated protein, TIGR03984 family. Members of this protein family are found exclusively in CRISPR-containing organisms, in operon contexts with RAMP (repeat-associated mystery protein) proteins also linked to CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats).
2PRK110451848135.81.3E+02[                      ------------------------   ]pagPphospholipid:lipid A palmitoyltransferase; Provisional
3PRK008012012235.421[               -----                             ]PRK00801hypothetical protein; Provisional
4cd034441044231.81E+02[         -----------                             ]Thioesterase_II_repeat1Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.
5pfam110042813127.036[               --------                          ]Kdo_hydroxy3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) hydroxylase. This is a family of 3-deoxy-D-manno-oct-2-ulosonic acid 3-hydroxylases, which catalyse the conversion of 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) to D-glycero-D-talo-oct-2-ulosonic acid (Ko). It contains a potential iron-binding motif, HXDX(n)H (n>40). Hydroxylation activity is iron-dependent.
6pfam13511601823.938[                                         ----    ]DUF4124Domain of unknown function (DUF4124). This presumed domain is found in a variety of bacterial proteins. It is found associated at the N-terminus associated with other domains such as the SLT domain and glutaredoxin domains in some proteins. The function of this domain is unknown, but it may have an Ig-like fold.
7cd060631463422.332[           ---------                             ]H2MP_Cyano-H2upThis group of endopeptidases include HupW enzymes that are specific to the cyanobacterial hydrogenase and are involved in the C-terminal cleavage of the hydrogenase large subunit precursor protein. Cyanobacterial nickel-iron (NiFe)-hydrogenases are found exclusively in the N2-fixing strains and are encoded by hup (hydrogen uptake) genes. These uptake hydrogenases are heterodimers with a large (hupL) and small subunit (hupS) and catalyze the consumption of the H2 produced during N2 fixation. Sequence similarity shows that the putative metal-binding resides are well conserved in this group of hydrogen maturation proteases. This group also includes such proteins as the hydrogenase III from Aquifex aeolicus.
8pfam123951111520.474[                   ----                          ]DUF3658Protein of unknown function. This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam08874. There are two completely conserved residues (D and R) that may be functionally important.
9pfam070171478020.03.2E+02[                      ------------------------   ]PagPAntimicrobial peptide resistance and lipid A acylation protein PagP. This family consists of several bacterial antimicrobial peptide resistance and lipid A acylation (PagP) proteins. The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic antimicrobial peptides produced during the host innate immune response.
10pfam03778201117.785[                    ---                          ]DUF321Protein of unknown function (DUF321). This family may be related to the FARP (FMRFamide) family, pfam01581. Currently this repeat was only detectable in Arabidopsis thaliana.