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Conserved domains on  [gi|1722471813|gb|QED26898|]
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SGNH/GDSL hydrolase family protein [Microvenator marinus]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10083122)

SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity

CATH:  3.40.50.1110
EC:  3.1.-.-
Gene Ontology:  GO:0016788
PubMed:  35871440|15522763
SCOP:  3001315

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 154-360 2.10e-22

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: 93.25  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSI----PVFGPTPYFPNILRDKFQRFG-EVTLENVAVSGSTSVEWIPGavhFENRLSPNLGEADLIVFSLGGND 228
Cdd:cd00229     1 ILVIGDSItagyGASSGSTFYSLLLYLLLLAGGpGVEVINLGVSGATTADALRR---LGLRLALLKDKPDLVIIELGTND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 229 LQDFAFEIdpnnvaakigelpalIDEIEANLKLTIAEVRAQNPDADIVWLVYPNYARSTEWEAFIPPQNKELAVRFldst 308
Cdd:cd00229    78 LGRGGDTS---------------IDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAV---- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1722471813 309 lsdVRKRMANEDILLLDMLGATAEENLDTFLVDPLHLNVEGHQFWADELFRL 360
Cdd:cd00229   139 ---AAENPAPSGVDLVDLAALLGDEDKSLYSPDGIHPNPAGHKLIAEALASA 187
 
Name Accession Description Interval E-value
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 154-360 2.10e-22

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: 93.25  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSI----PVFGPTPYFPNILRDKFQRFG-EVTLENVAVSGSTSVEWIPGavhFENRLSPNLGEADLIVFSLGGND 228
Cdd:cd00229     1 ILVIGDSItagyGASSGSTFYSLLLYLLLLAGGpGVEVINLGVSGATTADALRR---LGLRLALLKDKPDLVIIELGTND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 229 LQDFAFEIdpnnvaakigelpalIDEIEANLKLTIAEVRAQNPDADIVWLVYPNYARSTEWEAFIPPQNKELAVRFldst 308
Cdd:cd00229    78 LGRGGDTS---------------IDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAV---- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1722471813 309 lsdVRKRMANEDILLLDMLGATAEENLDTFLVDPLHLNVEGHQFWADELFRL 360
Cdd:cd00229   139 ---AAENPAPSGVDLVDLAALLGDEDKSLYSPDGIHPNPAGHKLIAEALASA 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 154-362 2.46e-20

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: 87.78  E-value: 2.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSIPV-FGPTPY--FPNILRDKFQRfGEVTLENVAVSGSTSVEWIpgavhfeNRLSPNL--GEADLIVFSLGGND 228
Cdd:COG2755    11 IVALGDSITAgYGASRErgWPALLARRLAA-ADVRVVNAGISGATTADLL-------ARLDRDLlaLKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 229 LQDfAFEIDPnnvaakigelpaliDEIEANLKLTIAEVRAQNPDADIVWLVYPNYARSTEWEAFIPPQNKELavrfldst 308
Cdd:COG2755    83 LLR-GLGVSP--------------EEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAI-------- 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1722471813 309 lsdvrKRMANE-DILLLDMLGATAEEN--LDTFLVDPLHLNVEGHQFWADELFRLLG 362
Cdd:COG2755   140 -----RELAAEyGVPLVDLYAALRDAGdlPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 156-351 7.27e-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: 71.81  E-value: 7.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 156 VFGDSI--------PVFGPTPYFPNILRDKFQRFGEVtleNVAVSGSTSVEWIPGAVHFENRLSPnlgeaDLIVFSLGGN 227
Cdd:pfam13472   1 ALGDSItagygatgGDRSYPGWLARLLARRLGADVVN---NLGISGATTRLDLLERLDDVLRLKP-----DLVVILLGTN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 228 DLqdfAFEIDPnnvaakigelpaliDEIEANLKLTIAEVRAQNPDADIV-WLVYPNYARSTEWEAFIPPQNKELAVRfld 306
Cdd:pfam13472  73 DL---GRGVSA--------------ARAAANLEALIDALRAAGPDARVLlIGPLPVGPPPPLDERRLNARIAEYNAA--- 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1722471813 307 stlsdVRKRMANEDILLLDMLGATAEENL---DTFLVDPLHLNVEGHQ 351
Cdd:pfam13472 133 -----IREVAAERGVPYVDLWDALRDDGGwlpDLLADDGLHPNAAGYR 175
 
Name Accession Description Interval E-value
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 154-360 2.10e-22

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: 93.25  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSI----PVFGPTPYFPNILRDKFQRFG-EVTLENVAVSGSTSVEWIPGavhFENRLSPNLGEADLIVFSLGGND 228
Cdd:cd00229     1 ILVIGDSItagyGASSGSTFYSLLLYLLLLAGGpGVEVINLGVSGATTADALRR---LGLRLALLKDKPDLVIIELGTND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 229 LQDFAFEIdpnnvaakigelpalIDEIEANLKLTIAEVRAQNPDADIVWLVYPNYARSTEWEAFIPPQNKELAVRFldst 308
Cdd:cd00229    78 LGRGGDTS---------------IDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAV---- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1722471813 309 lsdVRKRMANEDILLLDMLGATAEENLDTFLVDPLHLNVEGHQFWADELFRL 360
Cdd:cd00229   139 ---AAENPAPSGVDLVDLAALLGDEDKSLYSPDGIHPNPAGHKLIAEALASA 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 154-362 2.46e-20

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: 87.78  E-value: 2.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSIPV-FGPTPY--FPNILRDKFQRfGEVTLENVAVSGSTSVEWIpgavhfeNRLSPNL--GEADLIVFSLGGND 228
Cdd:COG2755    11 IVALGDSITAgYGASRErgWPALLARRLAA-ADVRVVNAGISGATTADLL-------ARLDRDLlaLKPDLVVIELGTND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 229 LQDfAFEIDPnnvaakigelpaliDEIEANLKLTIAEVRAQNPDADIVWLVYPNYARSTEWEAFIPPQNKELavrfldst 308
Cdd:COG2755    83 LLR-GLGVSP--------------EEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAI-------- 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1722471813 309 lsdvrKRMANE-DILLLDMLGATAEEN--LDTFLVDPLHLNVEGHQFWADELFRLLG 362
Cdd:COG2755   140 -----RELAAEyGVPLVDLYAALRDAGdlPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 156-351 7.27e-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: 71.81  E-value: 7.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 156 VFGDSI--------PVFGPTPYFPNILRDKFQRFGEVtleNVAVSGSTSVEWIPGAVHFENRLSPnlgeaDLIVFSLGGN 227
Cdd:pfam13472   1 ALGDSItagygatgGDRSYPGWLARLLARRLGADVVN---NLGISGATTRLDLLERLDDVLRLKP-----DLVVILLGTN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 228 DLqdfAFEIDPnnvaakigelpaliDEIEANLKLTIAEVRAQNPDADIV-WLVYPNYARSTEWEAFIPPQNKELAVRfld 306
Cdd:pfam13472  73 DL---GRGVSA--------------ARAAANLEALIDALRAAGPDARVLlIGPLPVGPPPPLDERRLNARIAEYNAA--- 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1722471813 307 stlsdVRKRMANEDILLLDMLGATAEENL---DTFLVDPLHLNVEGHQ 351
Cdd:pfam13472 133 -----IREVAAERGVPYVDLWDALRDDGGwlpDLLADDGLHPNAAGYR 175
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
154-357 6.19e-13

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 67.21  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSIPVF---GPTPYF--PNILRDKFQRF------GEVTLENVAVSGSTSVEWIPGAVHFENRLSPNLGEA--DLI 220
Cdd:pfam00657   1 IVAFGDSLTDGggdGPGGRFswGDLLADFLARKlgvpgsGYNHGANFAIGGATIEDLPIQLEQLLRLISDVKDQAkpDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 221 VFSLGGNDLqdFAFEIDPNNVAAKIGELpalIDEIEANLKLTIAEVRAQNPDADIVWLVYPNYarstEWEAFIPPQNKEL 300
Cdd:pfam00657  81 TIFIGANDL--CNFLSSPARSKKRVPDL---LDELRANLPQLGLGARKFWVHGLGPLGCTPPK----GCYELYNALAEEY 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 301 AvRFLDSTLSDVRKRMANEDILLLDMLGATAEENLDT---FLVDPLHLNVEGHQFWADEL 357
Cdd:pfam00657 152 N-ERLNELVNSLAAAAEDANVVYVDIYGFEDPTDPCCgigLEPDGLHPSEKGYKAVAEAI 210
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 154-361 4.42e-09

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: 55.21  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSIPV-FGPTPY--FPNILRDKFQRFG-EVTLENVAVSGSTSVewipGAVhfeNRLSPNL--GEADLIVFSLGGN 227
Cdd:cd01822     3 ILALGDSLTAgYGLPPEegWPALLQKRLDARGiDVTVINAGVSGDTTA----GGL---ARLPALLaqHKPDLVILELGGN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 228 D-LQDFAfeidpnnvaakigelpalIDEIEANLKLTIAEVRAQNpdADIV---WLVYPNYAR--STEWEAFIPPQNKELA 301
Cdd:cd01822    76 DgLRGIP------------------PDQTRANLRQMIETAQARG--APVLlvgMQAPPNYGPryTRRFAAIYPELAEEYG 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 302 VRFLDSTLSDVRKRMAnediLLLDmlgataeenldtflvDPLHLNVEGHQFWADELFRLL 361
Cdd:cd01822   136 VPLVPFFLEGVAGDPE----LMQS---------------DGIHPNAEGQPIIAENVWPAL 176
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 170-355 8.48e-08

SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this 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, but may lack the carboxylic acid.


Pssm-ID: 238861  Cd Length: 259  Bit Score: 52.84  E-value: 8.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 170 FPNILRdkfQRFGEV--TLENVAVSGSTSVEWIPGAVHFENRLSPNLGEA-DLIVFSLGGNDL----------QDFAFEI 236
Cdd:cd01823    34 YPTLLA---RALGDEtlSFTDVACSGATTTDGIEPQQGGIAPQAGALDPDtDLVTITIGGNDLgfadvvkaciLTGGGSS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 237 DPNNVAAKIGELPALIDEIEANLKLTIAEVRAQNPDADIVWLVYPNY--------ARSTEWEAFIPPQNKELAVRF---L 305
Cdd:cd01823   111 LAQEKGAADGARDAALDEVGARLKAVLDRIRERAPNARVVVVGYPRLfppdggdcDKSCSPGTPLTPADRPELNQLvdkL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722471813 306 DSTLSDVRKRMANEDILLLDMLGATA--------------EENLDTFLVDPLHLNVEGHQFWAD 355
Cdd:cd01823   191 NALIRRAAADAGDYKVRFVDTDAPFAghracspdpwsrsvLDLLPTRQGKPFHPNAAGHRAIAD 254
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 154-360 5.07e-07

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: 49.57  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSIPV-FG--PTPYFPNILRDKF-----QRFGEVTLENVAVSGSTSVEWIPGAVHFENRLSPnlgeaDLIVFSLG 225
Cdd:cd01832     2 YVALGDSITEgVGdpVPDGGYRGWADRLaaalaAADPGIEYANLAVRGRRTAQILAEQLPAALALRP-----DLVTLLAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 226 GNDLqdFAFEIDPnnvaakigelpaliDEIEANLKLTIAEVRAqnPDADIVWLVYPNYArstEWEAFIPPQNKELAvrfl 305
Cdd:cd01832    77 GNDI--LRPGTDP--------------DTYRADLEEAVRRLRA--AGARVVVFTIPDPA---VLEPFRRRVRARLA---- 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1722471813 306 dsTLSDVRKRMANE-DILLLDMLGATAEENLDTFLVDPLHLNVEGHQFWADELFRL 360
Cdd:cd01832   132 --AYNAVIRAVAARyGAVHVDLWEHPEFADPRLWASDRLHPSAAGHARLAALVLAA 185
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 154-329 5.28e-07

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: 49.58  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSipvFGPTPYFPNILRDkfqRFGeVTLENVAVSGSTSVEW--IPGAVHfENRLSPnlGEADLIVFSLGGNDLQD 231
Cdd:cd01825     2 IAQLGDS---HIAGDFFTDVLRG---LLG-VIYDNLGVNGASASLLlkWDAEFL-QAQLAA--LPPDLVILSYGTNEAFN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 232 FAFEidpnnvaakigelpalIDEIEANLKLTIAEVRAQNPDADIVWLVYPNYARSTEWEAFIPPqnkelaVRFldSTLSD 311
Cdd:cd01825    72 KQLN----------------ASEYRQQLREFIKRLRQILPNASILLVGPPDSLQKTGAGRWRTP------PGL--DAVIA 127

                         170
                  ....*....|....*....
gi 1722471813 312 VRKRMANE-DILLLDMLGA 329
Cdd:cd01825   128 AQRRVAKEeGIAFWDLYAA 146
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 153-351 8.09e-07

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: 48.83  E-value: 8.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 153 DILVF-GDSIP-VFGPTPYFPNILRDKFQRFgEVTLENVAVSGSTsvewipgAVHFENRLSPNLG--EADLIVFSLGGND 228
Cdd:cd01834     2 DRIVFiGNSITdRGGYVGYVETYLAARYPEL-KLTFRNLGWSGDT-------VSDLAARRDRDVLpaKPDVVSIMFGIND 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 229 LqdFAFEIDPNNvaakigelpalIDEIEANLKLTIAEVRAQNPDADIVwLVYPN-YARSTEWEAFIPPQNKELAvrflds 307
Cdd:cd01834    74 S--FRGFDDPVG-----------LEKFKTNLRRLIDRLKNKESAPRIV-LVSPIaYEANEDPLPDGAEYNANLA------ 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1722471813 308 TLSDVRKRMANED-ILLLD----MLGATAEENLDTFLVDPLHLNVEGHQ 351
Cdd:cd01834   134 AYADAVRELAAENgVAFVDlftpMKEAFQKAGEAVLTVDGVHPNEAGHR 182
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 153-357 8.93e-07

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: 48.43  E-value: 8.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 153 DILVFGDSIPVFGPTPyfpnilrdkfQRFGEVTLENVAVSGSTSVEwipgavhFENRLSPNL-GEADLIVFSLGGNDLQD 231
Cdd:cd01828     1 ALVFLGDSLTEGGPWA----------LLFPDVKVANRGISGDTTRG-------LLARLDEDVaLQPKAIFIMIGINDLAQ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 232 FAfeidpnnvaakigelpaLIDEIEANLKLTIAEVRAQNPDADI-VWLVYPNYARSTEWEAFIPPQNKELA-------VR 303
Cdd:cd01828    64 GT-----------------SDEDIVANYRTILEKLRKHFPNIKIvVQSILPVGELKSIPNEQIEELNRQLAqlaqqegVT 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1722471813 304 FLD--STLSDVRKRMANEdillldmlgataeenldtFLVDPLHLNVEGHQFWADEL 357
Cdd:cd01828   127 FLDlwAVFTNADGDLKNE------------------FTTDGLHLNAKGYAVWAAAL 164
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 165-278 1.40e-06

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. This subfamily contains sequences similar to Bacillus YpmR.


Pssm-ID: 239947  Cd Length: 204  Bit Score: 48.40  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 165 GPTPYFPNILRDKFQRfgEVTLENVAVSGSTSVEwipgavhFENRLS-----PNLGEADLIVFSLGGNDLQDFAFEIDPN 239
Cdd:cd04506    21 GYVGRLDKLIETKTVK--KVTVQNFGVSGDRSDQ-------LLKRLKtkkvqKELKKADVITITIGGNDLMQVLEKNFLS 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1722471813 240 NVAAKI--GELPAlideiEANLKLTIAEVRAQNPDADIVWL 278
Cdd:cd04506    92 LDVEDFkkAEETY-----QNNLKKIFKEIRKLNPDAPIFLV 127
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 154-361 5.35e-06

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: 46.86  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSIPVFGPTPYFP---NILRDKFQRFGEVtlENVAVSGSTSvEWipgAVHFENR--LSPNLGEADLIVFSLGGND 228
Cdd:cd01838     2 IVLFGDSITQFSFDQGEFgfgAALADVYSRKLDV--INRGFSGYNT-RW---ALKVLPKifLEEKLAQPDLVTIFFGAND 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 229 LQDFAFeidPNNVaakigelpaLIDEIEANLKLTIAEVRAQNPDADIVwLVYPNYARSTEWEAFIPPQNKELaVRFLDST 308
Cdd:cd01838    76 AALPGQ---PQHV---------PLDEYKENLRKIVSHLKSLSPKTKVI-LITPPPVDEEAWEKSLEDGGSQP-GRTNELL 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1722471813 309 L--SDVRKRMANE-DILLLDMLGATAEEN--LDTFLVDPLHLNVEGHQFWADELFRLL 361
Cdd:cd01838   142 KqyAEACVEVAEElGVPVIDLWTAMQEEAgwLESLLTDGLHFSSKGYELLFEEIVKVI 199
Endoglucanase_E_like cd01831
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
 217-357 3.41e-04

Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.


Pssm-ID: 238869  Cd Length: 169  Bit Score: 40.79  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 217 ADLIVFSLGGNDlqdFAFEIDPNNvaakigelpaliDEIEANLKLTIAEVRAQNPDADIVWLVYPNYArsteweafiPPQ 296
Cdd:cd01831    56 PDLVVINLGTND---FSTGNNPPG------------EDFTNAYVEFIEELRKRYPDAPIVLMLGPMLF---------GPY 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722471813 297 NKELAVrfldSTLSDVRKRMANEDILLLDMLGATAEENLDtflvDPLHLNVEGHQFWADEL 357
Cdd:cd01831   112 GTEEEI----KRVAEAFKDQKSKKVHYFDTPGILQHNDIG----CDWHPTVAGHQKIAKHL 164
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 216-355 1.47e-03

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: 38.76  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 216 EADLIVFSLGGNDlqdfafeIDPNNVAAKIGE-LPALIDEIeanlkltiaevRAQNPDADIVWL-VYPNyaRSTEWEAFI 293
Cdd:cd01833    40 KPDVVLLHLGTND-------LVLNRDPDTAPDrLRALIDQM-----------RAANPDVKIIVAtLIPT--TDASGNARI 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722471813 294 PPQNKELAvrfldSTLSDvrKRMANEDILLLDMLGATaeeNLDTFLVDPLHLNVEGHQFWAD 355
Cdd:cd01833   100 AEYNAAIP-----GVVAD--LRTAGSPVVLVDMSTGY---TTADDLYDGLHPNDQGYKKMAD 151
fatty_acyltransferase_like cd01846
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ...
 154-359 4.67e-03

Fatty acyltransferase-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. Might catalyze fatty acid transfer between phosphatidylcholine and sterols.


Pssm-ID: 238882 [Multi-domain]  Cd Length: 270  Bit Score: 38.51  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 154 ILVFGDSI------------PVFGPTPYFPN-----------ILRDKFQRFGEVTLENVAVSGSTSVEWIPGAVH----- 205
Cdd:cd01846     2 LVVFGDSLsdtgnifkltggSNPPPSPPYFGgrfsngpvwveYLAATLGLSGLKQGYNYAVGGATAGAYNVPPYPptlpg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 206 -------FENRLSPNLGEADLIVFSLGGNDL-QDFAFEIDPNNVAAKIgelpalIDEIEANLKlTIAEVRAQNpdadIVW 277
Cdd:cd01846    82 lsdqvaaFLAAHKLRLPPDTLVAIWIGANDLlNALDLPQNPDTLVTRA------VDNLFQALQ-RLYAAGARN----FLV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722471813 278 LVYPNYARSTeweAFIPPQNKELAV---------RFLDSTLSDVRKRMANEDILLLDM---------------------- 326
Cdd:cd01846   151 LNLPDLGLTP---AFQAQGDAVAARataltaaynAKLAEKLAELKAQHPGVNILLFDTnalfndildnpaaygftnvtdp 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1722471813 327 --------LGATAEENLDTFLV-DPLHLNVEGHQFWADELFR 359
Cdd:cd01846   228 cldyvysySPREACANPDKYLFwDEVHPTTAVHQLIAEEVAA 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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