|
Name |
Accession |
Description |
Interval |
E-value |
| SGNH_hydrolase_like_7 |
cd04502 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
70-241 |
2.01e-96 |
|
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: 239946 Cd Length: 171 Bit Score: 280.33 E-value: 2.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 70 GVLFVGSSTIRLWTDLREDFRQLPVvINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQSF 149
Cdd:cd04502 1 GILFYGSSSIRLWDTLADDLAPLPV-VNRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTPEEVLRDFREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 150 VRSVREALPDTRISYISIKPSPLRLSLLPRMREANALLAQYVRTVPNSDFIDIFTPMLDAQGLPRAELFGADHLHMNDAG 229
Cdd:cd04502 80 VNRIRAKLPDTPIAIISIKPSPARWALRPKIRRFNALLKELAETRPNLTYIDVASPMLDADGKPRAELFQEDGLHLNDAG 159
|
170
....*....|..
gi 2129694995 230 YDLWRAVIGSYV 241
Cdd:cd04502 160 YALWRKVIKPAL 171
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
62-242 |
4.05e-30 |
|
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: 111.66 E-value: 4.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 62 KAGLPKAGGVLFVGSSTIRLWTD---------LREDFRQLPV-VINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDN 131
Cdd:COG2755 2 KAAAGKPLRIVALGDSITAGYGAsrergwpalLARRLAAADVrVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 132 DLAEGR--TPEQVLESFQSFVRSVREALPDTRISYISIKPSPLRLSLLPRMREANALLAQYVRTvPNSDFIDIFTPMLDA 209
Cdd:COG2755 82 DLLRGLgvSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAIRELAAE-YGVPLVDLYAALRDA 160
|
170 180 190
....*....|....*....|....*....|...
gi 2129694995 210 QGLPraELFGADHLHMNDAGYDLWRAVIGSYVG 242
Cdd:COG2755 161 GDLP--DLLTADGLHPNAAGYRLIAEAVLPALK 191
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
70-232 |
1.53e-18 |
|
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: 80.67 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 70 GVLFVGSSTIRLWTDLREDFRQLPVVINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQSF 149
Cdd:pfam13472 11 GATGGDRSYPGWLARLLARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSAARAAANLEAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 150 VRSVREALPDTRISYISIKP-SPLRLSLLPRMREANALLAQYVRTV---PNSDFIDIFTPMLDaQGLPRAELFGADHLHM 225
Cdd:pfam13472 91 IDALRAAGPDARVLLIGPLPvGPPPPLDERRLNARIAEYNAAIREVaaeRGVPYVDLWDALRD-DGGWLPDLLADDGLHP 169
|
....*..
gi 2129694995 226 NDAGYDL 232
Cdd:pfam13472 170 NAAGYRL 176
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SGNH_hydrolase_like_7 |
cd04502 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
70-241 |
2.01e-96 |
|
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: 239946 Cd Length: 171 Bit Score: 280.33 E-value: 2.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 70 GVLFVGSSTIRLWTDLREDFRQLPVvINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQSF 149
Cdd:cd04502 1 GILFYGSSSIRLWDTLADDLAPLPV-VNRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTPEEVLRDFREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 150 VRSVREALPDTRISYISIKPSPLRLSLLPRMREANALLAQYVRTVPNSDFIDIFTPMLDAQGLPRAELFGADHLHMNDAG 229
Cdd:cd04502 80 VNRIRAKLPDTPIAIISIKPSPARWALRPKIRRFNALLKELAETRPNLTYIDVASPMLDADGKPRAELFQEDGLHLNDAG 159
|
170
....*....|..
gi 2129694995 230 YDLWRAVIGSYV 241
Cdd:cd04502 160 YALWRKVIKPAL 171
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
62-242 |
4.05e-30 |
|
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: 111.66 E-value: 4.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 62 KAGLPKAGGVLFVGSSTIRLWTD---------LREDFRQLPV-VINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDN 131
Cdd:COG2755 2 KAAAGKPLRIVALGDSITAGYGAsrergwpalLARRLAAADVrVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 132 DLAEGR--TPEQVLESFQSFVRSVREALPDTRISYISIKPSPLRLSLLPRMREANALLAQYVRTvPNSDFIDIFTPMLDA 209
Cdd:COG2755 82 DLLRGLgvSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAIRELAAE-YGVPLVDLYAALRDA 160
|
170 180 190
....*....|....*....|....*....|...
gi 2129694995 210 QGLPraELFGADHLHMNDAGYDLWRAVIGSYVG 242
Cdd:COG2755 161 GDLP--DLLTADGLHPNAAGYRLIAEAVLPALK 191
|
|
| sialate_O-acetylesterase_like2 |
cd01828 |
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ... |
71-237 |
1.21e-27 |
|
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: 104.28 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 71 VLFVGSStIRLWTDLREDFRQLPVViNRGFGGSTMADCqYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQSFV 150
Cdd:cd01828 2 LVFLGDS-LTEGGPWALLFPDVKVA-NRGISGDTTRGL-LARLDEDVALQPKAIFIMIGINDLAQGTSDEDIVANYRTIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 151 RSVREALPDTRISYISIKPSPLRLSLLPR-MREANALLAQYVRTvPNSDFIDIFTPMLDAQGLPRAElFGADHLHMNDAG 229
Cdd:cd01828 79 EKLRKHFPNIKIVVQSILPVGELKSIPNEqIEELNRQLAQLAQQ-EGVTFLDLWAVFTNADGDLKNE-FTTDGLHLNAKG 156
|
....*...
gi 2129694995 230 YDLWRAVI 237
Cdd:cd01828 157 YAVWAAAL 164
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
70-232 |
1.53e-18 |
|
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: 80.67 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 70 GVLFVGSSTIRLWTDLREDFRQLPVVINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQSF 149
Cdd:pfam13472 11 GATGGDRSYPGWLARLLARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSAARAAANLEAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 150 VRSVREALPDTRISYISIKP-SPLRLSLLPRMREANALLAQYVRTV---PNSDFIDIFTPMLDaQGLPRAELFGADHLHM 225
Cdd:pfam13472 91 IDALRAAGPDARVLLIGPLPvGPPPPLDERRLNARIAEYNAAIREVaaeRGVPYVDLWDALRD-DGGWLPDLLADDGLHP 169
|
....*..
gi 2129694995 226 NDAGYDL 232
Cdd:pfam13472 170 NAAGYRL 176
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
71-240 |
9.89e-18 |
|
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: 78.61 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 71 VLFVGSSTIRLWTDLREDFRQLP-------------VVINRGFGGSTMADCQYFVKN--LVLQYQPRHVMVYAGDNDLAE 135
Cdd:cd00229 1 ILVIGDSITAGYGASSGSTFYSLllyllllaggpgvEVINLGVSGATTADALRRLGLrlALLKDKPDLVIIELGTNDLGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 136 G--RTPEQVLESFQSFVRSVREALPDTRISYISIKPSPLRL----SLLPRMREANALLAQYVRTVPNSDFIDIFTPMLDA 209
Cdd:cd00229 81 GgdTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREgllgRALPRYNEAIKAVAAENPAPSGVDLVDLAALLGDE 160
|
170 180 190
....*....|....*....|....*....|.
gi 2129694995 210 qglpRAELFGADHLHMNDAGYDLWRAVIGSY 240
Cdd:cd00229 161 ----DKSLYSPDGIHPNPAGHKLIAEALASA 187
|
|
| NnaC_like |
cd01841 |
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ... |
69-241 |
1.03e-13 |
|
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: 67.35 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 69 GGVLFVGSSTIRLWtDLREDFRQLPVVINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQS 148
Cdd:cd01841 1 KNIVFIGDSLFEGW-PLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSSNQFIKWYRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 149 FVRSVREALPDTRISYISIKPSPLRLSLLPRMRE----ANALLaQYVRTVPNSDFIDIFTPMLDAQGlPRAELFGADHLH 224
Cdd:cd01841 80 IIEQIREEFPNTKIYLLSVLPVLEEDEIKTRSNTriqrLNDAI-KELAPELGVTFIDLNDVLVDEFG-NLKKEYTTDGLH 157
|
170
....*....|....*..
gi 2129694995 225 MNDAGYDLWRAVIGSYV 241
Cdd:cd01841 158 FNPKGYQKLLEILEEYL 174
|
|
| PAF_acetylesterase_like |
cd01820 |
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ... |
49-233 |
1.88e-13 |
|
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction.
Pssm-ID: 238858 Cd Length: 214 Bit Score: 67.70 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 49 RWQSSMDAFAAADKAGLPKaggVLFVGSSTIRLW--TDL---REDFRQLPVvINRGFGGSTMADCQYFVKNLVLQY-QPR 122
Cdd:cd01820 16 RWMSRHERFVAEAKQKEPD---VVFIGDSITQNWefTGLevwRELYAPLHA-LNFGIGGDRTQNVLWRLENGELDGvNPK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 123 HVMVYAGDNDLAEGRTPEQVLESFQSFVRSVREALPDTRISYISI-----KPSPLRLsllpRMREANALLAQYVRTVPNS 197
Cdd:cd01820 92 VVVLLIGTNNIGHTTTAEEIAEGILAIVEEIREKLPNAKILLLGLlprgqNPNPLRE----RNAQVNRLLAVRYDGLPNV 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 2129694995 198 DFIDIFTPMLDAQGLPRAELFgADHLHMNDAGYDLW 233
Cdd:cd01820 168 TFLDIDKGFVQSDGTISHHDM-PDYLHLTAAGYRKW 202
|
|
| XynB_like |
cd01833 |
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ... |
97-237 |
8.87e-13 |
|
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. 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: 238871 Cd Length: 157 Bit Score: 64.56 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 97 NRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQSFVRSVREALPDTRISYISIKPSPLRlSL 176
Cdd:cd01833 17 HEGHSGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNRDPDTAPDRLRALIDQMRAANPDVKIIVATLIPTTDA-SG 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2129694995 177 LPRMREANALLAQYVRTVPNSD----FIDIFTPMLDAQGLpraelfgADHLHMNDAGY----DLWRAVI 237
Cdd:cd01833 96 NARIAEYNAAIPGVVADLRTAGspvvLVDMSTGYTTADDL-------YDGLHPNDQGYkkmaDAWYEAL 157
|
|
| Isoamyl_acetate_hydrolase_like |
cd01838 |
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ... |
95-233 |
2.00e-12 |
|
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: 64.20 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 95 VINRGFGGSTMADCQYFVKNLVL---QYQPRHVMVYAGDNDLAEGRTPEQV-LESFQS----FVRSVREALPDTRIsyIS 166
Cdd:cd01838 35 VINRGFSGYNTRWALKVLPKIFLeekLAQPDLVTIFFGANDAALPGQPQHVpLDEYKEnlrkIVSHLKSLSPKTKV--IL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 167 IKPSPLRLSLLPRMREA--------NALLAQY---VRTVP---NSDFIDIFTPMLDAQGLPRAELfgADHLHMNDAGYDL 232
Cdd:cd01838 113 ITPPPVDEEAWEKSLEDggsqpgrtNELLKQYaeaCVEVAeelGVPVIDLWTAMQEEAGWLESLL--TDGLHFSSKGYEL 190
|
.
gi 2129694995 233 W 233
Cdd:cd01838 191 L 191
|
|
| SGNH_hydrolase_like_2 |
cd01834 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
71-230 |
3.60e-12 |
|
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: 63.47 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 71 VLFVGSSTI-------RLWTDLREDFRQLPV-VINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQV 142
Cdd:cd01834 4 IVFIGNSITdrggyvgYVETYLAARYPELKLtFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDSFRGFDDPVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 143 LESFQS----FVRSVREALPDTRISYISikPSPLRLSLLPRMREA--NALLAQYVRTV-----PNS-DFIDIFTPMLDAQ 210
Cdd:cd01834 84 LEKFKTnlrrLIDRLKNKESAPRIVLVS--PIAYEANEDPLPDGAeyNANLAAYADAVrelaaENGvAFVDLFTPMKEAF 161
|
170 180
....*....|....*....|
gi 2129694995 211 GLPRAELFGADHLHMNDAGY 230
Cdd:cd01834 162 QKAGEAVLTVDGVHPNEAGH 181
|
|
| SGNH_hydrolase_like_4 |
cd04501 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
82-232 |
1.82e-11 |
|
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: 61.19 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 82 WTDLREDFRQLPVvINRGFGGSTMADCQYFVKNLVLQYQPRHVMVYAGDNDLAEGRTPEQVLESFQSFVRSVREAlpdtr 161
Cdd:cd04501 22 WVNLLAEFLGKEV-INRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNTSLEMIKDNIRSMVELAEAN----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 162 isyiSIKP---SPLRLSLLP----------RMREANALLAQYVRTVpNSDFIDIFTPMLDAQGLPRAELFGADHLHMNDA 228
Cdd:cd04501 96 ----GIKVilaSPLPVDDYPwkpqwlrpanKLKSLNRWLKDYAREN-GLLFLDFYSPLLDERNVGLKPGLLTDGLHPSRE 170
|
....
gi 2129694995 229 GYDL 232
Cdd:cd04501 171 GYRV 174
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
55-230 |
4.17e-05 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 43.33 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 55 DAFAAADKAGlpkAGGVLFVGSSTIRLWTD-LREDFRQLPVVINRGFGGSTMADCQYFVKNLV-------LQYQPRHVMV 126
Cdd:pfam00657 6 DSLTDGGGDG---PGGRFSWGDLLADFLARkLGVPGSGYNHGANFAIGGATIEDLPIQLEQLLrlisdvkDQAKPDLVTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 127 YAGDNDLAEGR-TPEQVLESFQSFVRSVREALPDTRISY----------ISIKPSPLRLSLLPRMREA-NALLAQYVR-- 192
Cdd:pfam00657 83 FIGANDLCNFLsSPARSKKRVPDLLDELRANLPQLGLGArkfwvhglgpLGCTPPKGCYELYNALAEEyNERLNELVNsl 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2129694995 193 -------TVPNSDFIDIFTPMLDAQGLPraelFGADHLHMNDAGY 230
Cdd:pfam00657 163 aaaaedaNVVYVDIYGFEDPTDPCCGIG----LEPDGLHPSEKGY 203
|
|
| SGNH_hydrolase_like_6 |
cd01844 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
95-232 |
9.66e-04 |
|
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: 238881 Cd Length: 177 Bit Score: 39.23 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129694995 95 VINRGFGGSTMADcqYFVKNLVLQYQPRHVMVYAGDNDLAEGRTpeqVLESFQSFVRSVREALPDTRISYISIKPSPLRL 174
Cdd:cd01844 34 VINLGFSGNARLE--PEVAELLRDVPADLYIIDCGPNIVGAEAM---VRERLGPLVKGLRETHPDTPILLVSPRYCPDAE 108
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129694995 175 sLLPRMREAN-----ALLAQYVR----TVPNSDFIDIFTpMLDAQGLPRaelfgADHLHMNDAGYDL 232
Cdd:cd01844 109 -LTPGRGKLTlavrrALREAFEKlradGVPNLYYLDGEE-LLGPDGEAL-----VDGIHPTDLGHMR 168
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