|
Name |
Accession |
Description |
Interval |
E-value |
| XynE_like |
cd01830 |
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ... |
216-412 |
7.07e-111 |
|
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. 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: 238868 Cd Length: 204 Bit Score: 323.81 E-value: 7.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 216 TVVALGDSITDGDKSTTSTNRRWPNLLASRILAGPKPHQFGVMNAGISGNRVLADGPGVSAQARFDRDVLAQPDVSTVVV 295
Cdd:cd01830 1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 296 MEGVNDLRW------ELATKPADLIQAYRQLIGRAHARGVCIVGGTITPWEGGSLWSEPKDAIRGEVNAWIRTSGEFDAV 369
Cdd:cd01830 81 LEGVNDIGAsgtdfaAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATRQAVNEWIRTSGAFDAV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497462330 370 VDFDAAVRDPAQPSRILAAYDSGDHLHPGDAGYQAMANAVDLD 412
Cdd:cd01830 161 VDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLD 203
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
210-409 |
1.95e-38 |
|
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: 137.08 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 210 APQQVDTVVALGDSITDGdkSTTSTNRRWPNLLASRIlagpKPHQFGVMNAGISGNRVLadgpgvSAQARFDRDVLA-QP 288
Cdd:COG2755 4 AAGKPLRIVALGDSITAG--YGASRERGWPALLARRL----AAADVRVVNAGISGATTA------DLLARLDRDLLAlKP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 289 DVstVVVMEGVNDLRWELATKPADLIQAYRQLIGRAHARG--VCIVGGTITPWeggsLWSEPKDAIRGEVNAWIRTSG-E 365
Cdd:COG2755 72 DL--VVIELGTNDLLRGLGVSPEEFRANLEALIDRLRAAGpgARVVLVTPPPR----LRPNYLNERIEAYNAAIRELAaE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497462330 366 FDA-VVDFDAAVRDPAQpsriLAAYDSGDHLHPGDAGYQAMANAV 409
Cdd:COG2755 146 YGVpLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
219-404 |
1.17e-27 |
|
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: 108.02 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 219 ALGDSITDGdKSTTSTNRRWPNLLASRILAgpKPHQFGVMNAGISGNRVLADGPGvsaqaRFDRDVLAQPDVstVVVMEG 298
Cdd:pfam13472 1 ALGDSITAG-YGATGGDRSYPGWLARLLAR--RLGADVVNNLGISGATTRLDLLE-----RLDDVLRLKPDL--VVILLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 299 VNDLRWelATKPADLIQAYRQLIGRAHARG--VCIVGGTITPWEG-GSLWSEPKDAIRGEVNAWIRTSGEFD--AVVDFD 373
Cdd:pfam13472 71 TNDLGR--GVSAARAAANLEALIDALRAAGpdARVLLIGPLPVGPpPPLDERRLNARIAEYNAAIREVAAERgvPYVDLW 148
|
170 180 190
....*....|....*....|....*....|.
gi 497462330 374 AAVRDPAQPsriLAAYDSGDHLHPGDAGYQA 404
Cdd:pfam13472 149 DALRDDGGW---LPDLLADDGLHPNAAGYRL 176
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| XynE_like |
cd01830 |
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ... |
216-412 |
7.07e-111 |
|
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. 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: 238868 Cd Length: 204 Bit Score: 323.81 E-value: 7.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 216 TVVALGDSITDGDKSTTSTNRRWPNLLASRILAGPKPHQFGVMNAGISGNRVLADGPGVSAQARFDRDVLAQPDVSTVVV 295
Cdd:cd01830 1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 296 MEGVNDLRW------ELATKPADLIQAYRQLIGRAHARGVCIVGGTITPWEGGSLWSEPKDAIRGEVNAWIRTSGEFDAV 369
Cdd:cd01830 81 LEGVNDIGAsgtdfaAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATRQAVNEWIRTSGAFDAV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497462330 370 VDFDAAVRDPAQPSRILAAYDSGDHLHPGDAGYQAMANAVDLD 412
Cdd:cd01830 161 VDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLD 203
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
210-409 |
1.95e-38 |
|
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: 137.08 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 210 APQQVDTVVALGDSITDGdkSTTSTNRRWPNLLASRIlagpKPHQFGVMNAGISGNRVLadgpgvSAQARFDRDVLA-QP 288
Cdd:COG2755 4 AAGKPLRIVALGDSITAG--YGASRERGWPALLARRL----AAADVRVVNAGISGATTA------DLLARLDRDLLAlKP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 289 DVstVVVMEGVNDLRWELATKPADLIQAYRQLIGRAHARG--VCIVGGTITPWeggsLWSEPKDAIRGEVNAWIRTSG-E 365
Cdd:COG2755 72 DL--VVIELGTNDLLRGLGVSPEEFRANLEALIDRLRAAGpgARVVLVTPPPR----LRPNYLNERIEAYNAAIRELAaE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497462330 366 FDA-VVDFDAAVRDPAQpsriLAAYDSGDHLHPGDAGYQAMANAV 409
Cdd:COG2755 146 YGVpLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
219-404 |
1.17e-27 |
|
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: 108.02 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 219 ALGDSITDGdKSTTSTNRRWPNLLASRILAgpKPHQFGVMNAGISGNRVLADGPGvsaqaRFDRDVLAQPDVstVVVMEG 298
Cdd:pfam13472 1 ALGDSITAG-YGATGGDRSYPGWLARLLAR--RLGADVVNNLGISGATTRLDLLE-----RLDDVLRLKPDL--VVILLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 299 VNDLRWelATKPADLIQAYRQLIGRAHARG--VCIVGGTITPWEG-GSLWSEPKDAIRGEVNAWIRTSGEFD--AVVDFD 373
Cdd:pfam13472 71 TNDLGR--GVSAARAAANLEALIDALRAAGpdARVLLIGPLPVGPpPPLDERRLNARIAEYNAAIREVAAERgvPYVDLW 148
|
170 180 190
....*....|....*....|....*....|.
gi 497462330 374 AAVRDPAQPsriLAAYDSGDHLHPGDAGYQA 404
Cdd:pfam13472 149 DALRDDGGW---LPDLLADDGLHPNAAGYRL 176
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
217-409 |
3.96e-25 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 101.88 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 217 VVALGDSITDGDKSTTSTNRRWPNLLASRI---LAGPKPHQFGVMNAGISGNRVLADGPGVSAQARFDRDVLAQPDVSTV 293
Cdd:pfam00657 1 IVAFGDSLTDGGGDGPGGRFSWGDLLADFLarkLGVPGSGYNHGANFAIGGATIEDLPIQLEQLLRLISDVKDQAKPDLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 294 VVMEGVNDLRWELATKP----------ADLIQAYRQLIGRAHARGVC---IVGGTITPWEGGSLWSEPKDaIRGEVNAWI 360
Cdd:pfam00657 81 TIFIGANDLCNFLSSPArskkrvpdllDELRANLPQLGLGARKFWVHglgPLGCTPPKGCYELYNALAEE-YNERLNELV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497462330 361 RTSGEF---DAVVDFDAAvrDPAQPSRILAAYDSG-DHLHPGDAGYQAMANAV 409
Cdd:pfam00657 160 NSLAAAaedANVVYVDIY--GFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
|
|
| SGNH_hydrolase_like_4 |
cd04501 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
217-410 |
2.36e-19 |
|
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: 85.07 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 217 VVALGDSITDG--DKSTTStnrrWPNLLAsrilagpKPHQFGVMNAGISGNrvladgpgVSAQ--ARFDRDVLA-QPDVs 291
Cdd:cd04501 3 VVCLGDSITYGypVGPEAS----WVNLLA-------EFLGKEVINRGINGD--------TTSQmlVRFYEDVIAlKPAV- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 292 tVVVMEGVNDLRWElaTKPADLIQAYRQLIGRAHARGVCIVGGTITP-----WEGGslWSEPKDAIRgEVNAWI----RT 362
Cdd:cd04501 63 -VIIMGGTNDIIVN--TSLEMIKDNIRSMVELAEANGIKVILASPLPvddypWKPQ--WLRPANKLK-SLNRWLkdyaRE 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497462330 363 SGEFdaVVDFDAAVRDPAQPSRILAAYDsgDHLHPGDAGYQAMANAVD 410
Cdd:cd04501 137 NGLL--FLDFYSPLLDERNVGLKPGLLT--DGLHPSREGYRVMAPLAE 180
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
217-409 |
1.07e-16 |
|
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: 77.84 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 217 VVALGDSITDGDKSTtSTNRRWPNLLASRILAGPKPHQfgVMNAGISGNRVLAdgpGVSAQARFDRDVLAQPDVstVVVM 296
Cdd:cd00229 1 ILVIGDSITAGYGAS-SGSTFYSLLLYLLLLAGGPGVE--VINLGVSGATTAD---ALRRLGLRLALLKDKPDL--VIIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 297 EGVNDLRWELATKPADLIQAYRQLIGRAHAR--GVCIVGGTITP----WEGGSLWSEPKDAIRGEVNAWIRtSGEFDAVV 370
Cdd:cd00229 73 LGTNDLGRGGDTSIDEFKANLEELLDALRERapGAKVILITPPPppprEGLLGRALPRYNEAIKAVAAENP-APSGVDLV 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 497462330 371 DFDAAVRDPaqpsriLAAYDSGDHLHPGDAGYQAMANAV 409
Cdd:cd00229 152 DLAALLGDE------DKSLYSPDGIHPNPAGHKLIAEAL 184
|
|
| SGNH_hydrolase_like_2 |
cd01834 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
215-408 |
3.30e-14 |
|
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: 70.78 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 215 DTVVALGDSITDGdksttstnRRWPNLLASRILAGPKPHQFGVMNAGISGNRVlADGPgvsaqARFDRDVL-AQPDVstV 293
Cdd:cd01834 2 DRIVFIGNSITDR--------GGYVGYVETYLAARYPELKLTFRNLGWSGDTV-SDLA-----ARRDRDVLpAKPDV--V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 294 VVMEGVNDLR--WELATKPADLIQAYRQLIGRAH--ARGVCIVGGTITPWEGGSLWS---EPKDAIRGEVNAWIRTSG-E 365
Cdd:cd01834 66 SIMFGINDSFrgFDDPVGLEKFKTNLRRLIDRLKnkESAPRIVLVSPIAYEANEDPLpdgAEYNANLAAYADAVRELAaE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497462330 366 FDA-VVDFDAAVRDpaqpsrILAAYDSG----DHLHPGDAGYQAMANA 408
Cdd:cd01834 146 NGVaFVDLFTPMKE------AFQKAGEAvltvDGVHPNEAGHRALARL 187
|
|
| XynB_like |
cd01833 |
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ... |
217-408 |
1.99e-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: 67.65 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 217 VVALGDSITDGDKSttstnrrwpnllasrilagpkphqfgvmNAGISGNRVladgpGVSAQARFDRDVLAQPDVstVVVM 296
Cdd:cd01833 3 IMPLGDSITWGDKD----------------------------HEGHSGYLI-----DQIAAAAADWVLAAKPDV--VLLH 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 297 EGVNDLRWElaTKPADLIQAYRQLIG--RAHARGVCIVGGTITPWEGGSL---WSEPKDAIRGEVNAWiRTSGEFDAVVD 371
Cdd:cd01833 48 LGTNDLVLN--RDPDTAPDRLRALIDqmRAANPDVKIIVATLIPTTDASGnarIAEYNAAIPGVVADL-RTAGSPVVLVD 124
|
170 180 190
....*....|....*....|....*....|....*..
gi 497462330 372 fdaavrdpaQPSRILAAYDSGDHLHPGDAGYQAMANA 408
Cdd:cd01833 125 ---------MSTGYTTADDLYDGLHPNDQGYKKMADA 152
|
|
| Lysophospholipase_L1_like |
cd01822 |
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ... |
215-409 |
3.55e-12 |
|
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.
Pssm-ID: 238860 [Multi-domain] Cd Length: 177 Bit Score: 64.46 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 215 DTVVALGDSITDG-----DKSttstnrrWPNLLASRILAGPKPHQfgVMNAGISGNrvladgpgVSAQ--ARFDRdVLAQ 287
Cdd:cd01822 1 VTILALGDSLTAGyglppEEG-------WPALLQKRLDARGIDVT--VINAGVSGD--------TTAGglARLPA-LLAQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 288 PDVSTVVVMEGVNDLrweLATKPADLIQA-YRQLIGRAHARG--VCIVGGTITPWEGGSLWSEPkDAIRGEVnawirtSG 364
Cdd:cd01822 63 HKPDLVILELGGNDG---LRGIPPDQTRAnLRQMIETAQARGapVLLVGMQAPPNYGPRYTRRF-AAIYPEL------AE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497462330 365 EFDAVV--DFDAAVRDpaQPSRILAaydsgDHLHPGDAGYQAMANAV 409
Cdd:cd01822 133 EYGVPLvpFFLEGVAG--DPELMQS-----DGIHPNAEGQPIIAENV 172
|
|
| sialate_O-acetylesterase_like2 |
cd01828 |
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ... |
217-409 |
1.11e-08 |
|
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: 54.21 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 217 VVALGDSITDGdksttstnrrWPNLLAsrilagpkPHQFGVMNAGISGNRVlaDGpgvsAQARFDRDVLAQPDvsTVVVM 296
Cdd:cd01828 2 LVFLGDSLTEG----------GPWALL--------FPDVKVANRGISGDTT--RG----LLARLDEDVALQPK--AIFIM 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 297 EGVNDLRWElaTKPADLIQAYRQLIG--RAHARGVCIVGGTITPweGGSLWSEPKDAIRgEVN----AWIRTSGEfdAVV 370
Cdd:cd01828 56 IGINDLAQG--TSDEDIVANYRTILEklRKHFPNIKIVVQSILP--VGELKSIPNEQIE-ELNrqlaQLAQQEGV--TFL 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 497462330 371 DFDAAVRDpaqPSRILAAYDSGDHLHPGDAGYQAMANAV 409
Cdd:cd01828 129 DLWAVFTN---ADGDLKNEFTTDGLHLNAKGYAVWAAAL 164
|
|
| SGNH_hydrolase_like_1 |
cd01832 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
217-409 |
9.31e-08 |
|
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: 51.89 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 217 VVALGDSITDG--DKSTTSTNRRWPNLLASRILAGPKPhqFGVMNAGISGNR---VLADGPGVSAQARFDRdvlaqpdvs 291
Cdd:cd01832 2 YVALGDSITEGvgDPVPDGGYRGWADRLAAALAAADPG--IEYANLAVRGRRtaqILAEQLPAALALRPDL--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497462330 292 tVVVMEGVNDL---RWELATKPADLIQAYRQLigRAHARGVCIVggTITPWEGGSLWSEPKDAIRGEVNAWIRT-SGEFD 367
Cdd:cd01832 71 -VTLLAGGNDIlrpGTDPDTYRADLEEAVRRL--RAAGARVVVF--TIPDPAVLEPFRRRVRARLAAYNAVIRAvAARYG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497462330 368 AV-VDFDA--AVRDPaqpsrilaAYDSGDHLHPGDAGYQAMANAV 409
Cdd:cd01832 146 AVhVDLWEhpEFADP--------RLWASDRLHPSAAGHARLAALV 182
|
|
| |
