match no.	target id	target length	alignment length	probability	E-value	coverage	match description
1	pfam08386	103	102	99.9	5.9E-28	[ ----------]	Abhydrolase_4	TAP-like protein. This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.
2	pfam00561	225	76	99.5	1.2E-13	[ ------------ ]	Abhydrolase_1	alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.
3	pfam12697	224	43	99.0	2.3E-09	[ ----- ]	Abhydrolase_6	Alpha/beta hydrolase family. This family contains alpha/beta hydrolase enzymes of diverse specificity.
4	COG0596	282	101	99.0	2.1E-10	[ --------------- ]	MhpC	Pimeloyl-ACP methyl ester carboxylesterase
5	pfam12695	145	39	98.3	2.1E-06	[ --- ]	Abhydrolase_5	Alpha/beta hydrolase family. This family contains a diverse range of alpha/beta hydrolase enzymes.
6	COG2267	298	177	97.5	0.00047	[ ----------------------- ]	PldB	Lysophospholipase, alpha-beta hydrolase superfamily
7	TIGR01249	306	131	97.5	0.00017	[ ------------------ ]	pro_imino_pep_1	proline iminopeptidase, Neisseria-type subfamily. This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.
8	PRK08775	343	49	96.2	0.0021	[ ----- ]	PRK08775	homoserine O-acetyltransferase; Provisional
9	TIGR03695	252	78	95.8	0.0037	[ ------------ ]	menH_SHCHC	2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase.
10	TIGR01250	289	131	95.7	0.031	[ ----------------- ]	pro_imino_pep_2	proline-specific peptidase, Bacillus coagulans-type subfamily. This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase
11	TIGR03611	248	221	95.0	0.02	[ ------------------------------------- ]	RutD	pyrimidine utilization protein D. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the hydrolase, alpha/beta fold family defined by pfam00067.
12	COG4757	281	104	93.5	0.058	[ --------------- ]	COG4757	Predicted alpha/beta hydrolase
13	TIGR03343	282	107	92.8	0.048	[ --------------- ]	biphenyl_bphD	2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase. Members of this family are 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, or HOPD hydrolase, the BphD protein of biphenyl degradation. BphD acts on the product of ring meta-cleavage by BphC. Many species carrying bphC and bphD are capable of degrading polychlorinated biphenyls as well as biphenyl itself.
14	TIGR02427	251	48	92.5	0.2	[ ----- ]	protocat_pcaD	3-oxoadipate enol-lactonase. Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate.
15	COG2939	498	80	91.1	0.68	[ -------- ]	Kex1	Carboxypeptidase C (cathepsin A)
16	PRK14875	371	77	90.9	0.099	[ --------- ]	PRK14875	acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
17	COG2021	368	211	88.8	0.24	[ --------------------------- ]	MET2	Homoserine acetyltransferase
18	COG1506	620	125	87.7	0.39	[ ---------------- ]	DAP2	Dipeptidyl aminopeptidase/acylaminoacyl peptidase
19	cd00741	153	26	87.7	0.39	[ -- ]	Lipase	Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
20	TIGR01738	245	128	87.3	0.65	[ ------------------ ]	bioH	pimelyl-
21	TIGR01392	351	56	85.6	0.44	[ ----- ]	homoserO_Ac_trn	homoserine O-acetyltransferase. This family describes homoserine-O-acetyltransferase, an enzyme of methionine biosynthesis. This model has been rebuilt to identify sequences more broadly, including a number of sequences suggested to be homoserine O-acetyltransferase based on proximity to other Met biosynthesis genes.
22	COG2945	210	22	85.4	0.71	[ -- ]	COG2945	Alpha/beta superfamily hydrolase
23	pfam00326	212	44	84.2	0.59	[ ----- ]	Peptidase_S9	Prolyl oligopeptidase family.
24	PRK03592	295	44	83.2	0.55	[ ---- ]	PRK03592	haloalkane dehalogenase; Provisional
25	PRK07581	339	57	82.6	0.8	[ ----- ]	PRK07581	hypothetical protein; Validated
26	PRK10673	255	76	79.2	0.94	[ ------------ ]	PRK10673	acyl-CoA esterase; Provisional
27	COG3243	445	41	76.1	1.6	[ ---- ]	PhaC	Poly(3-hydroxyalkanoate) synthetase
28	COG1647	243	55	75.6	1.4	[ ----- ]	YvaK	Esterase/lipase
29	pfam12146	80	46	74.9	3.6	[ ----- ]	Hydrolase_4	Putative lysophospholipase. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. Many members are annotated as being lysophospholipases, and others as alpha-beta hydrolase fold-containing proteins.
30	TIGR03100	274	24	74.9	1.7	[ -- ]	hydr1_PEP	exosortase A system-associated hydrolase 1. This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 2, TIGR03101) of the same superfamily.
31	PRK10349	256	104	73.1	3.7	[ --------------- ]	PRK10349	carboxylesterase BioH; Provisional
32	PRK00175	379	221	72.4	1.9	[ --------------------------- ]	metX	homoserine O-acetyltransferase; Provisional
33	pfam08840	211	46	69.0	9.4	[ ---- ]	BAAT_C	BAAT / Acyl-CoA thioester hydrolase C terminal. This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).
34	pfam00975	224	56	68.5	4.4	[ ------- ]	Thioesterase	Thioesterase domain. Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
35	cd12808	309	27	68.0	2	[ -- ]	Esterase_713_like-1	Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds. This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
36	COG0412	236	36	67.3	2.6	[ ---- ]	DLH	Dienelactone hydrolase
37	pfam05057	212	14	65.1	2.6	[ -- ]	DUF676	Putative serine esterase (DUF676). This family of proteins are probably serine esterase type enzymes with an alpha/beta hydrolase fold.
38	cd00519	229	28	60.9	5.2	[ --- ]	Lipase_3	Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
39	PRK11126	242	77	59.6	11	[ ------------- ]	PRK11126	2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
40	TIGR01250	289	41	58.5	11	[ ----- ]	pro_imino_pep_2	proline-specific peptidase, Bacillus coagulans-type subfamily. This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase
41	TIGR03056	278	42	56.6	14	[ ---- ]	bchO_mg_che_rel	putative magnesium chelatase accessory protein. Members of this family belong to the alpha/beta fold family hydrolases (pfam00561). Members are found in bacterial genomes if and only if they encoded for anoxygenic photosynthetic systems similar to that of Rhodobacter capsulatus and other alpha-Proteobacteria. Members often are encoded in the same operon as subunits of the protoporphyrin IX magnesium chelatase, and were once designated BchO. No literature supports a role as an actual subunit of magnesium chelatase, but an accessory role is possible, as suggested by placement by its probable hydrolase activity.
42	pfam00326	212	32	56.1	20	[ --- ]	Peptidase_S9	Prolyl oligopeptidase family.
43	pfam06028	249	31	53.4	8.7	[ --- ]	DUF915	Alpha/beta hydrolase of unknown function (DUF915). This family consists of several bacterial proteins of unknown function. Members of this family have an alpha/beta hydrolase fold.
44	pfam11144	403	30	53.0	6.2	[ --- ]	DUF2920	Protein of unknown function (DUF2920). This bacterial family of proteins has no known function.
45	TIGR02427	251	43	51.9	18	[ ---- ]	protocat_pcaD	3-oxoadipate enol-lactonase. Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate.
46	COG0596	282	57	51.3	30	[ ------ ]	MhpC	Pimeloyl-ACP methyl ester carboxylesterase
47	TIGR02240	276	33	50.4	8.4	[ --- ]	PHA_depoly_arom	poly(3-hydroxyalkanoate) depolymerase. This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans, Pseudomonas putida BM01, and related species. This enzyme is part of polyester storage and mobilization system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on carbon sources such as benzoic acid or phenylacetic acid.
48	TIGR01836	350	54	49.2	9.3	[ ------- ]	PHA_synth_III_C	poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit. This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerize short-chain-length hydroxyalkanoates.
49	COG1073	299	41	48.5	29	[ --- ]	FrsA	Fermentation-respiration switch protein FrsA, has esterase activity, DUF1100 family
50	pfam01764	139	28	47.3	12	[ -- ]	Lipase_3	Lipase (class 3).
51	cd03720	42	14	47.2	9.4	[ - ]	SOCS_ASB1	SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.
52	COG0400	207	33	46.0	16	[ --- ]	YpfH	Predicted esterase
53	COG0657	312	53	45.3	16	[ ------ ]	Aes	Acetyl esterase/lipase
54	pfam02129	265	79	44.7	18	[ ------------ ]	Peptidase_S15	X-Pro dipeptidyl-peptidase (S15 family).
55	pfam05524	123	43	44.4	24	[ ----- ]	PEP-utilizers_N	PEP-utilizing enzyme, N-terminal.
56	cd00707	275	37	42.2	14	[ --- ]	Pancreat_lipase_like	Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
57	pfam06259	177	42	41.3	13	[ ---- ]	Abhydrolase_8	Alpha/beta hydrolase. Members of this family are predicted to have an alpha/beta hydrolase fold. They contain a predicted Ser-His-Asp catalytic triad, in which the serine is likely to act as a nucleophile.
58	cd07225	306	25	39.6	14	[ -- ]	Pat_PNPLA6_PNPLA7	Patatin-like phospholipase domain containing protein 6 and protein 7. Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologous to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster.
59	COG4188	365	46	39.2	15	[ ------- ]	COG4188	Predicted dienelactone hydrolase
60	pfam07819	225	27	37.8	34	[ --- ]	PGAP1	PGAP1-like protein. The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body.
61	PRK11071	190	82	36.4	24	[ ---------- ]	PRK11071	esterase YqiA; Provisional
62	PRK00148	194	59	34.8	75	[ ------ ]	PRK00148	Maf-like protein; Reviewed
63	TIGR02821	275	32	33.4	9.3	[ --- ]	fghA_ester_D	S-formylglutathione hydrolase. This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well.
64	pfam00756	246	31	30.5	26	[ --- ]	Esterase	Putative esterase. This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
65	pfam00205	137	47	29.7	84	[ ---- ]	TPP_enzyme_M	Thiamine pyrophosphate enzyme, central domain. The central domain of TPP enzymes contains a 2-fold Rossman fold.
66	pfam13768	155	109	29.1	23	[ ----------- ]	VWA_3	von Willebrand factor type A domain.
67	pfam10230	260	24	28.1	29	[ -- ]	DUF2305	Uncharacterized conserved protein (DUF2305). This family of proteins is conserved from plants to humans. The function is unknown.
68	TIGR03101	266	17	28.1	30	[ - ]	hydr2_PEP	exosortase A system-associated hydrolase 2. This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.
69	cd07228	175	33	27.1	29	[ --- ]	Pat_NTE_like_bacteria	Bacterial patatin-like phospholipase domain containing protein 6. Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens.
70	pfam10730	147	21	26.6	25	[ --]	DUF2521	Protein of unknown function (DUF2521). Family of unknown function specific to Bacillus.
71	COG3458	321	34	26.1	25	[ --- ]	Axe1	Cephalosporin-C deacetylase or related acetyl esterase
72	TIGR03123	318	79	25.9	33	[ --------]	one_C_unchar_1	probable H4MPT-linked C1 transfer pathway protein. This protein family was identified, by the method of partial phylogenetic profiling, as related to the use of tetrahydromethanopterin (H4MPT) as a C-1 carrier. Characteristic markers of the H4MPT-linked C1 transfer pathway include formylmethanofuran dehydrogenase subunits, methenyltetrahydromethanopterin cyclohydrolase, etc. Tetrahydromethanopterin, a tetrahydrofolate analog, occurs in methanogenic archaea, bacterial methanotrophs, planctomycetes, and a few other lineages.
73	COG2267	298	56	25.8	73	[ ------ ]	PldB	Lysophospholipase, alpha-beta hydrolase superfamily
74	cd12809	280	140	25.7	38	[ ---------------- ]	Esterase_713_like-2	Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds. This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
75	TIGR03695	252	41	25.5	31	[ ---- ]	menH_SHCHC	2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase.
76	TIGR03056	278	75	24.8	43	[ ------------ ]	bchO_mg_che_rel	putative magnesium chelatase accessory protein. Members of this family belong to the alpha/beta fold family hydrolases (pfam00561). Members are found in bacterial genomes if and only if they encoded for anoxygenic photosynthetic systems similar to that of Rhodobacter capsulatus and other alpha-Proteobacteria. Members often are encoded in the same operon as subunits of the protoporphyrin IX magnesium chelatase, and were once designated BchO. No literature supports a role as an actual subunit of magnesium chelatase, but an accessory role is possible, as suggested by placement by its probable hydrolase activity.
77	COG3411	64	40	23.7	60	[ ----]	2Fe2S	(2Fe-2S) ferredoxin
78	COG5607	283	176	22.6	4.6E+02	[ -------------------- ]	CHAD	CHAD domain (function unknown)
79	PRK05282	233	26	21.3	36	[ --- ]	PRK05282	(alpha)-aspartyl dipeptidase; Validated
80	COG4782	377	25	21.3	39	[ --- ]	COG4782	Esterase/lipase superfamily enzyme
81	cd03744	42	14	21.1	44	[ - ]	SOCS_SSB1	SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), both the absence and the presence of HGF and enhances the HGF-MET-induced mitogen-activated protein kinases Erk-transcription factor Elk-1-serum response elements (SRE) pathway. SSB1, like SSB2 and SSB4, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.
82	cd01466	155	54	21.0	62	[ ----- ]	vWA_C3HC4_type	VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.
83	pfam12695	145	48	20.1	1.1E+02	[ ----- ]	Abhydrolase_5	Alpha/beta hydrolase family. This family contains a diverse range of alpha/beta hydrolase enzymes.