|
Name |
Accession |
Description |
Interval |
E-value |
| Isoamyl_acetate_hydrolase_like |
cd01838 |
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ... |
39-221 |
9.88e-60 |
|
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
Pssm-ID: 238876 Cd Length: 199 Bit Score: 187.07 E-value: 9.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 39 RLTIIGDSITQKGFTPG--GYCAELMNFYQRRLRVDVWGFSGYTSRHVLRYLPEIPLE--IDSTKLLIVFLGTNDCQLTE 114
Cdd:cd01838 1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEekLAQPDLVTIFFGANDAALPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 115 TGYMCPVDEFKNNLLALTR----PFPHSKIIIVSPGICT-------------KDICFKREQEPYVIAASETVNTLNkska 177
Cdd:cd01838 81 QPQHVPLDEYKENLRKIVShlksLSPKTKVILITPPPVDeeaweksledggsQPGRTNELLKQYAEACVEVAEELG---- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19075953 178 nsAGLINLYEITKSYP-TPELLFTDGLHFSSLGYSLLFNEIVATI 221
Cdd:cd01838 157 --VPVIDLWTAMQEEAgWLESLLTDGLHFSSKGYELLFEEIVKVI 199
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
39-221 |
2.11e-19 |
|
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 82.77 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 39 RLTIIGDSITQkgftpgGYCAELMNFYQRRL---------RVDVWGFSGYTSRHVLRYLPEIPLEIDsTKLLIVFLGTND 109
Cdd:COG2755 10 RIVALGDSITA------GYGASRERGWPALLarrlaaadvRVVNAGISGATTADLLARLDRDLLALK-PDLVVIELGTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 110 CQlteTGYMCPVDEFKNNLLAL----TRPFPHSKIIIVSPGICTKDICFKREQEPYVIAASETVntlnksKANSAGLINL 185
Cdd:COG2755 83 LL---RGLGVSPEEFRANLEALidrlRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAIRELA------AEYGVPLVDL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 19075953 186 YEITKSYPT-PELLFTDGLHFSSLGYSLLFNEIVATI 221
Cdd:COG2755 154 YAALRDAGDlPDLLTADGLHPNAAGYRLIAEAVLPAL 190
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
40-217 |
6.18e-18 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 79.15 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 40 LTIIGDSITQKGFTPGG----YCAELMNFYQRRLRVDVWGFSGYTS---------------RHVLRYLPEIPLeIDSTKL 100
Cdd:pfam00657 1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPGSGYNHGANfaiggatiedlpiqlEQLLRLISDVKD-QAKPDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 101 LIVFLGTND-------CQLTETGYMCPVDEFKNNLLALTRPF----PHSKIIIVSPGICTKDICFKREQEPYVIAASETV 169
Cdd:pfam00657 80 VTIFIGANDlcnflssPARSKKRVPDLLDELRANLPQLGLGArkfwVHGLGPLGCTPPKGCYELYNALAEEYNERLNELV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19075953 170 NTLNKSKAN-SAGLINLYEITKSYPTPELLFT--DGLHFSSLGYSLLFNEI 217
Cdd:pfam00657 160 NSLAAAAEDaNVVYVDIYGFEDPTDPCCGIGLepDGLHPSEKGYKAVAEAI 210
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Isoamyl_acetate_hydrolase_like |
cd01838 |
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ... |
39-221 |
9.88e-60 |
|
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
Pssm-ID: 238876 Cd Length: 199 Bit Score: 187.07 E-value: 9.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 39 RLTIIGDSITQKGFTPG--GYCAELMNFYQRRLRVDVWGFSGYTSRHVLRYLPEIPLE--IDSTKLLIVFLGTNDCQLTE 114
Cdd:cd01838 1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEekLAQPDLVTIFFGANDAALPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 115 TGYMCPVDEFKNNLLALTR----PFPHSKIIIVSPGICT-------------KDICFKREQEPYVIAASETVNTLNkska 177
Cdd:cd01838 81 QPQHVPLDEYKENLRKIVShlksLSPKTKVILITPPPVDeeaweksledggsQPGRTNELLKQYAEACVEVAEELG---- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19075953 178 nsAGLINLYEITKSYP-TPELLFTDGLHFSSLGYSLLFNEIVATI 221
Cdd:cd01838 157 --VPVIDLWTAMQEEAgWLESLLTDGLHFSSKGYELLFEEIVKVI 199
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
39-221 |
2.11e-19 |
|
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 82.77 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 39 RLTIIGDSITQkgftpgGYCAELMNFYQRRL---------RVDVWGFSGYTSRHVLRYLPEIPLEIDsTKLLIVFLGTND 109
Cdd:COG2755 10 RIVALGDSITA------GYGASRERGWPALLarrlaaadvRVVNAGISGATTADLLARLDRDLLALK-PDLVVIELGTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 110 CQlteTGYMCPVDEFKNNLLAL----TRPFPHSKIIIVSPGICTKDICFKREQEPYVIAASETVntlnksKANSAGLINL 185
Cdd:COG2755 83 LL---RGLGVSPEEFRANLEALidrlRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAIRELA------AEYGVPLVDL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 19075953 186 YEITKSYPT-PELLFTDGLHFSSLGYSLLFNEIVATI 221
Cdd:COG2755 154 YAALRDAGDlPDLLTADGLHPNAAGYRLIAEAVLPAL 190
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
40-217 |
6.18e-18 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 79.15 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 40 LTIIGDSITQKGFTPGG----YCAELMNFYQRRLRVDVWGFSGYTS---------------RHVLRYLPEIPLeIDSTKL 100
Cdd:pfam00657 1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPGSGYNHGANfaiggatiedlpiqlEQLLRLISDVKD-QAKPDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 101 LIVFLGTND-------CQLTETGYMCPVDEFKNNLLALTRPF----PHSKIIIVSPGICTKDICFKREQEPYVIAASETV 169
Cdd:pfam00657 80 VTIFIGANDlcnflssPARSKKRVPDLLDELRANLPQLGLGArkfwVHGLGPLGCTPPKGCYELYNALAEEYNERLNELV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19075953 170 NTLNKSKAN-SAGLINLYEITKSYPTPELLFT--DGLHFSSLGYSLLFNEI 217
Cdd:pfam00657 160 NSLAAAAEDaNVVYVDIYGFEDPTDPCCGIGLepDGLHPSEKGYKAVAEAI 210
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
42-210 |
7.02e-15 |
|
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.
Pssm-ID: 463889 Cd Length: 176 Bit Score: 70.27 E-value: 7.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 42 IIGDSITQkGFTPGGYCAELMNFYQRRLR-------VDVWGFSGYTSRHVLRYLPEIPLEIDStKLLIVFLGTNDCqlte 114
Cdd:pfam13472 1 ALGDSITA-GYGATGGDRSYPGWLARLLArrlgadvVNNLGISGATTRLDLLERLDDVLRLKP-DLVVILLGTNDL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 115 tGYMCPVDEFKNNLLALTRPF----PHSKIIIVSPGICTKdicFKREQEPYVIAASETVNTLNKSKANSAG--LINLYEI 188
Cdd:pfam13472 75 -GRGVSAARAAANLEALIDALraagPDARVLLIGPLPVGP---PPPLDERRLNARIAEYNAAIREVAAERGvpYVDLWDA 150
|
170 180
....*....|....*....|....
gi 19075953 189 TKS--YPTPELLFTDGLHFSSLGY 210
Cdd:pfam13472 151 LRDdgGWLPDLLADDGLHPNAAGY 174
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
40-219 |
1.26e-14 |
|
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
Pssm-ID: 238141 [Multi-domain] Cd Length: 187 Bit Score: 69.75 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 40 LTIIGDSITQ-KGFTPGGYCAELMNFYQRRLRVDVW-----GFSGYTSRHVL-RYLPEIPLEIDSTKLLIVFLGTNDCQL 112
Cdd:cd00229 1 ILVIGDSITAgYGASSGSTFYSLLLYLLLLAGGPGVevinlGVSGATTADALrRLGLRLALLKDKPDLVIIELGTNDLGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 113 tetGYMCPVDEFKNNL----LALTRPFPHSKIIIVSPGICTKDICFKREQEPYVIAASETVNTLNKSKANsAGLINLYEI 188
Cdd:cd00229 81 ---GGDTSIDEFKANLeellDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENPAPSG-VDLVDLAAL 156
|
170 180 190
....*....|....*....|....*....|.
gi 19075953 189 TKSYPtPELLFTDGLHFSSLGYSLLFNEIVA 219
Cdd:cd00229 157 LGDED-KSLYSPDGIHPNPAGHKLIAEALAS 186
|
|
| SGNH_hydrolase_like_2 |
cd01834 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
38-213 |
7.86e-09 |
|
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238872 Cd Length: 191 Bit Score: 53.84 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 38 NRLTIIGDSITQKgftpGGYCAELMNFYQRR---LRVDVW--GFSGYTSRHVLRylPEIPLEID-STKLLIVFLGTND-- 109
Cdd:cd01834 2 DRIVFIGNSITDR----GGYVGYVETYLAARypeLKLTFRnlGWSGDTVSDLAA--RRDRDVLPaKPDVVSIMFGINDsf 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 110 CQLTETGYmcpVDEFKNNLLAL----TRPFPHSKIIIVSPGI---CTKDICFKREQEPYVIAASETVNTLnkSKANSAGL 182
Cdd:cd01834 76 RGFDDPVG---LEKFKTNLRRLidrlKNKESAPRIVLVSPIAyeaNEDPLPDGAEYNANLAAYADAVREL--AAENGVAF 150
|
170 180 190
....*....|....*....|....*....|....
gi 19075953 183 INLYEITK---SYPTPELLFTDGLHFSSLGYSLL 213
Cdd:cd01834 151 VDLFTPMKeafQKAGEAVLTVDGVHPNEAGHRAL 184
|
|
| FeeA_FeeB_like |
cd01836 |
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ... |
39-223 |
4.66e-07 |
|
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238874 Cd Length: 191 Bit Score: 48.80 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 39 RLTIIGDSI-------TQKGFTPGGYCAELMNFYQRRLRVDVWGFSGYTSRHVLRYLPEIPLEidSTKLLIVFLGTNDcq 111
Cdd:cd01836 4 RLLVLGDSTaagvgveTQDQALAGQLARGLAAITGRGVRWRLFAKTGATSADLLRQLAPLPET--RFDVAVISIGVND-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 112 lteTGYMCPVDEFKNNLL----ALTRPFPHSKIIIVS-PGICTkdicFKREQEP---YVIAASETVNTLNKSKANSAGLI 183
Cdd:cd01836 80 ---VTHLTSIARWRKQLAelvdALRAKFPGARVVVTAvPPLGR----FPALPQPlrwLLGRRARLLNRALERLASEAPRV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19075953 184 NLYEITkSYPTPELLFTDGLHFSSLGYSLLFNEIVATISK 223
Cdd:cd01836 153 TLLPAT-GPLFPALFASDGFHPSAAGYAVWAEALAPAIAA 191
|
|
| NnaC_like |
cd01841 |
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ... |
41-217 |
5.82e-06 |
|
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.
Pssm-ID: 238879 Cd Length: 174 Bit Score: 45.40 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 41 TIIGDSITQkGFtpggycaELMNFYQRRLRVDVWGFSGYTSRhvlRYLPEIPLEIDSTKLLIVFL--GTNDcqLTETGym 118
Cdd:cd01841 4 VFIGDSLFE-GW-------PLYEAEGKGKTVNNLGIAGISSR---QYLEHIEPQLIQKNPSKVFLflGTND--IGKEV-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 119 cPVDEFKNNLLAL----TRPFPHSKIIIVSPGICTKDICFKREQEPYVIAASETVNTLNKSKANSAGLINLYEITKSYPT 194
Cdd:cd01841 69 -SSNQFIKWYRDIieqiREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIQRLNDAIKELAPELGVTFIDLNDVLVDEFGNL 147
|
170 180
....*....|....*....|...
gi 19075953 195 PELLFTDGLHFSSLGYSLLFNEI 217
Cdd:cd01841 148 KKEYTTDGLHFNPKGYQKLLEIL 170
|
|
| SGNH_hydrolase_peri1 |
cd01825 |
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ... |
39-225 |
5.50e-05 |
|
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238863 Cd Length: 189 Bit Score: 42.65 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 39 RLTIIGDSITQKGFTPGGYCAELMNFYqrrlrvDVWGFSGYTSRhVLRYLPEIPLEIDS----TKLLIVFLGTNDCQLTE 114
Cdd:cd01825 1 RIAQLGDSHIAGDFFTDVLRGLLGVIY------DNLGVNGASAS-LLLKWDAEFLQAQLaalpPDLVILSYGTNEAFNKQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 115 TGYmcpvDEFKNNLLA----LTRPFPHSKIIIVSPGictkDICFKREQEPYVIAAS-ETVNTLNKSKANSAGLI--NLYE 187
Cdd:cd01825 74 LNA----SEYRQQLREfikrLRQILPNASILLVGPP----DSLQKTGAGRWRTPPGlDAVIAAQRRVAKEEGIAfwDLYA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19075953 188 I------TKSYPTPELLFTDGLHFSSLGYSLLFNEIVATISKAW 225
Cdd:cd01825 146 AmggeggIWQWAEPGLARKDYVHLTPRGYERLANLLYEALLKAY 189
|
|
| SGNH_hydrolase_like_1 |
cd01832 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
39-213 |
6.30e-04 |
|
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.
Pssm-ID: 238870 Cd Length: 185 Bit Score: 39.56 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 39 RLTIIGDSITQkGF----TPGGYC------AELMNFYQRRLRVDVWGFSGYTSRHVLryLPEIPLEIDSTKLLIVFL-GT 107
Cdd:cd01832 1 RYVALGDSITE-GVgdpvPDGGYRgwadrlAAALAAADPGIEYANLAVRGRRTAQIL--AEQLPAALALRPDLVTLLaGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 108 NDCQLTetgyMCPVDEFKNNLLALTRPF--PHSKIIIVSPGictkDIC----FKREQEPYVIAASEtvNTLNKSKANSAG 181
Cdd:cd01832 78 NDILRP----GTDPDTYRADLEEAVRRLraAGARVVVFTIP----DPAvlepFRRRVRARLAAYNA--VIRAVAARYGAV 147
|
170 180 190
....*....|....*....|....*....|..
gi 19075953 182 LINLYEITKSYpTPELLFTDGLHFSSLGYSLL 213
Cdd:cd01832 148 HVDLWEHPEFA-DPRLWASDRLHPSAAGHARL 178
|
|
| sialate_O-acetylesterase_like2 |
cd01828 |
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ... |
43-221 |
1.56e-03 |
|
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238866 Cd Length: 169 Bit Score: 38.03 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 43 IGDSITQkgftpGGYCAELMNFYQRRLRvdvwGFSGYTSRHVLRYLPEIpleIDSTKLLIVFL-GTNDcqlTETGYmcPV 121
Cdd:cd01828 5 LGDSLTE-----GGPWALLFPDVKVANR----GISGDTTRGLLARLDED---VALQPKAIFIMiGIND---LAQGT--SD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 122 DEFKNN----LLALTRPFPHSKIIIVS--PgictkdiCFKREQEPyviaaSETVNTLNK-----SKANSAGLINLYEI-- 188
Cdd:cd01828 68 EDIVANyrtiLEKLRKHFPNIKIVVQSilP-------VGELKSIP-----NEQIEELNRqlaqlAQQEGVTFLDLWAVft 135
|
170 180 190
....*....|....*....|....*....|....
gi 19075953 189 -TKSYPTPELlFTDGLHFSSLGYSLLFNEIVATI 221
Cdd:cd01828 136 nADGDLKNEF-TTDGLHLNAKGYAVWAAALQPYL 168
|
|
| SGNH_hydrolase_like_4 |
cd04501 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
38-221 |
3.34e-03 |
|
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
Pssm-ID: 239945 Cd Length: 183 Bit Score: 37.31 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 38 NRLTIIGDSITQkGFtPGGYCAELMNFYQRRLRVDVW--GFSGYTSRHVLRYLPEIPLEIDStKLLIVFLGTNDcqltet 115
Cdd:cd04501 1 MRVVCLGDSITY-GY-PVGPEASWVNLLAEFLGKEVInrGINGDTTSQMLVRFYEDVIALKP-AVVIIMGGTND------ 71
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075953 116 GYM-CPVDEFKNNLLAL-TRPFPH-SKIIIVSPgicTK-DIC-FKREQEPYVIAASETVNTLNK-SKANSAGLINLYEI- 188
Cdd:cd04501 72 IIVnTSLEMIKDNIRSMvELAEANgIKVILASP---LPvDDYpWKPQWLRPANKLKSLNRWLKDyARENGLLFLDFYSPl 148
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170 180 190
....*....|....*....|....*....|....*
gi 19075953 189 --TKSYPTPELLFTDGLHFSSLGYSLLFNEIVATI 221
Cdd:cd04501 149 ldERNVGLKPGLLTDGLHPSREGYRVMAPLAEKAL 183
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