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Conserved domains on  [gi|17534399|ref|NP_496841|]
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SGNH_hydro domain-containing protein [Caenorhabditis elegans]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110895)

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

 Zoom to residue level

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Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
fatty_acyltransferase_like cd01846
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ...
32-276 1.33e-44

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: 151.76  E-value: 1.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  32 RLIVFGDSLSDDGVEAEGESHGFL---------RNCNGKVWPEYVNAMLECDR---YVNYAYSGAKSGPGNF--YFDSFS 97
Cdd:cd01846   1 RLVVFGDSLSDTGNIFKLTGGSNPppsppyfggRFSNGPVWVEYLAATLGLSGlkqGYNYAVGGATAGAYNVppYPPTLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  98 GIQWQINQFLSNNKF-LSDDPLVILQTGGTIDFFGG------DTNSTEVVENIQQTIQNITqTMSTGTLVILSLLDVSNS 170
Cdd:cd01846  81 GLSDQVAAFLAAHKLrLPPDTLVAIWIGANDLLNALdlpqnpDTLVTRAVDNLFQALQRLY-AAGARNFLVLNLPDLGLT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399 171 PGVQAAEDSDilQERLGHLIAETNRQLHHIVLDSdlgtRRLNPFLRVRLIDINTVALAAMQ----------SLNTTEPFT 240
Cdd:cd01846 160 PAFQAQGDAV--AARATALTAAYNAKLAEKLAEL----KAQHPGVNILLFDTNALFNDILDnpaaygftnvTDPCLDYVY 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17534399 241 HHSPDLIPQAIYKYAYHDLWNPSTIVHYHIAKEIVR 276
Cdd:cd01846 234 SYSPREACANPDKYLFWDEVHPTTAVHQLIAEEVAA 269
 
Name Accession Description Interval E-value
fatty_acyltransferase_like cd01846
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ...
32-276 1.33e-44

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: 151.76  E-value: 1.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  32 RLIVFGDSLSDDGVEAEGESHGFL---------RNCNGKVWPEYVNAMLECDR---YVNYAYSGAKSGPGNF--YFDSFS 97
Cdd:cd01846   1 RLVVFGDSLSDTGNIFKLTGGSNPppsppyfggRFSNGPVWVEYLAATLGLSGlkqGYNYAVGGATAGAYNVppYPPTLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  98 GIQWQINQFLSNNKF-LSDDPLVILQTGGTIDFFGG------DTNSTEVVENIQQTIQNITqTMSTGTLVILSLLDVSNS 170
Cdd:cd01846  81 GLSDQVAAFLAAHKLrLPPDTLVAIWIGANDLLNALdlpqnpDTLVTRAVDNLFQALQRLY-AAGARNFLVLNLPDLGLT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399 171 PGVQAAEDSDilQERLGHLIAETNRQLHHIVLDSdlgtRRLNPFLRVRLIDINTVALAAMQ----------SLNTTEPFT 240
Cdd:cd01846 160 PAFQAQGDAV--AARATALTAAYNAKLAEKLAEL----KAQHPGVNILLFDTNALFNDILDnpaaygftnvTDPCLDYVY 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17534399 241 HHSPDLIPQAIYKYAYHDLWNPSTIVHYHIAKEIVR 276
Cdd:cd01846 234 SYSPREACANPDKYLFWDEVHPTTAVHQLIAEEVAA 269
COG3240 COG3240
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function ...
32-267 4.34e-20

Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 442472 [Multi-domain]  Cd Length: 305  Bit Score: 87.79  E-value: 4.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  32 RLIVFGDSLSDDG-------VEAEGESHGFLRNCNGKVWPEYVNAML------ECDRYVNYAYSGAKSGPGNFYFDSF-- 96
Cdd:COG3240  30 RIVVFGDSLSDTGnlfnltgGLPPSPPYFGGRFSNGPVWVEYLAAALglpltpSSAGGTNYAVGGARTGDGNGVLGGAal 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  97 -SGIQWQINQFL-SNNKFLSDDPLVILQTGGTiDFFGG----DTNSTEVVENIQQTIQNITQTMST------GTLVILSL 164
Cdd:COG3240 110 lPGLAQQVDAYLaAAGGTADPNALYIVWAGAN-DLLAAlaavGATPAQAQAAATAAAANLAAAVGAlaaagaRHILVPNL 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399 165 LDVSNSPGVQAAedSDILQERLGHLIAETNRQlhhivLDSDLGTRRLNpflrVRLIDINTVALAAMQSL------NTTEP 238
Cdd:COG3240 189 PDLGLTPAAQAL--GAAAAALLSALTAAFNQA-----LAAALPALGVN----IILFDVNSLFNEIIANPaaygftNVTDA 257
                       250       260       270
                ....*....|....*....|....*....|....
gi 17534399 239 FTHHSPDLI-----PQaiyKYAYHDLWNPSTIVH 267
Cdd:COG3240 258 CLSGTVSALlcvanPD---TYLFWDGVHPTTAAH 288
PRK15381 PRK15381
type III secretion system effector;
24-271 7.45e-07

type III secretion system effector;


Pssm-ID: 185279  Cd Length: 408  Bit Score: 49.66  E-value: 7.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399   24 RPRDFRCG---RLIVFGDSLSDDGVEAEGESHGFL---------RNCNGKVWPEYVNA-MLECDRYVNYAYSGAKSGPG- 89
Cdd:PRK15381 133 KPKNISLGditRLVFFGDSLSDSLGRMFEKTHHILpsygqyfggRFTNGFTWTEFLSSpHFLGKEMLNFAEGGSTSASYs 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399   90 --NFYFDSFSGIQWQINQFLSNNKFLSddpLVILqtgGTIDFFGGDTNSTEVVenIQQTIQNITQTMSTG--TLVILSLL 165
Cdd:PRK15381 213 cfNCIGDFVSNTDRQVASYTPSHQDLA---IFLL---GANDYMTLHKDNVIMV--VEQQIDDIEKIISGGvnNVLVMGIP 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  166 DVSNSP-GVQAAEDSDILQERLGHliaetNRQLHHIV--LDSDLGTRRLNPFLRVRLIDINTvALAAMQSLNTTEPFTHH 242
Cdd:PRK15381 285 DLSLTPyGKHSDEKRKLKDESIAH-----NALLKTNVeeLKEKYPQHKICYYETADAFKVIM-EAASNIGYDTENPYTHH 358
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 17534399  243 SPDLIPQA-------IYKYAYHDLWNPSTIVHYHIA 271
Cdd:PRK15381 359 GYVHVPGAkdpqldiCPQYVFNDLVHPTQEVHHCFA 394
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
33-197 1.31e-05

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 45.26  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399    33 LIVFGDSLSDDGveaeGEShGFLRNCNGKVWPEYVNAMLE-----CDRYVNYAYSGAKSGpgnfyfDSFSGIQwQINQFL 107
Cdd:pfam00657   1 IVAFGDSLTDGG----GDG-PGGRFSWGDLLADFLARKLGvpgsgYNHGANFAIGGATIE------DLPIQLE-QLLRLI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399   108 SNNKfLSDDPLVILQTGGTIDFFGGDTNSTEVVENIQQTIQNITQTM-----STGTLVILSLLDVSNSPGVQAAE----D 178
Cdd:pfam00657  69 SDVK-DQAKPDLVTIFIGANDLCNFLSSPARSKKRVPDLLDELRANLpqlglGARKFWVHGLGPLGCTPPKGCYElynaL 147
                         170
                  ....*....|....*....
gi 17534399   179 SDILQERLGHLIAETNRQL 197
Cdd:pfam00657 148 AEEYNERLNELVNSLAAAA 166
 
Name Accession Description Interval E-value
fatty_acyltransferase_like cd01846
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ...
32-276 1.33e-44

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: 151.76  E-value: 1.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  32 RLIVFGDSLSDDGVEAEGESHGFL---------RNCNGKVWPEYVNAMLECDR---YVNYAYSGAKSGPGNF--YFDSFS 97
Cdd:cd01846   1 RLVVFGDSLSDTGNIFKLTGGSNPppsppyfggRFSNGPVWVEYLAATLGLSGlkqGYNYAVGGATAGAYNVppYPPTLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  98 GIQWQINQFLSNNKF-LSDDPLVILQTGGTIDFFGG------DTNSTEVVENIQQTIQNITqTMSTGTLVILSLLDVSNS 170
Cdd:cd01846  81 GLSDQVAAFLAAHKLrLPPDTLVAIWIGANDLLNALdlpqnpDTLVTRAVDNLFQALQRLY-AAGARNFLVLNLPDLGLT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399 171 PGVQAAEDSDilQERLGHLIAETNRQLHHIVLDSdlgtRRLNPFLRVRLIDINTVALAAMQ----------SLNTTEPFT 240
Cdd:cd01846 160 PAFQAQGDAV--AARATALTAAYNAKLAEKLAEL----KAQHPGVNILLFDTNALFNDILDnpaaygftnvTDPCLDYVY 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17534399 241 HHSPDLIPQAIYKYAYHDLWNPSTIVHYHIAKEIVR 276
Cdd:cd01846 234 SYSPREACANPDKYLFWDEVHPTTAVHQLIAEEVAA 269
COG3240 COG3240
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function ...
32-267 4.34e-20

Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 442472 [Multi-domain]  Cd Length: 305  Bit Score: 87.79  E-value: 4.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  32 RLIVFGDSLSDDG-------VEAEGESHGFLRNCNGKVWPEYVNAML------ECDRYVNYAYSGAKSGPGNFYFDSF-- 96
Cdd:COG3240  30 RIVVFGDSLSDTGnlfnltgGLPPSPPYFGGRFSNGPVWVEYLAAALglpltpSSAGGTNYAVGGARTGDGNGVLGGAal 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  97 -SGIQWQINQFL-SNNKFLSDDPLVILQTGGTiDFFGG----DTNSTEVVENIQQTIQNITQTMST------GTLVILSL 164
Cdd:COG3240 110 lPGLAQQVDAYLaAAGGTADPNALYIVWAGAN-DLLAAlaavGATPAQAQAAATAAAANLAAAVGAlaaagaRHILVPNL 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399 165 LDVSNSPGVQAAedSDILQERLGHLIAETNRQlhhivLDSDLGTRRLNpflrVRLIDINTVALAAMQSL------NTTEP 238
Cdd:COG3240 189 PDLGLTPAAQAL--GAAAAALLSALTAAFNQA-----LAAALPALGVN----IILFDVNSLFNEIIANPaaygftNVTDA 257
                       250       260       270
                ....*....|....*....|....*....|....
gi 17534399 239 FTHHSPDLI-----PQaiyKYAYHDLWNPSTIVH 267
Cdd:COG3240 258 CLSGTVSALlcvanPD---TYLFWDGVHPTTAAH 288
PRK15381 PRK15381
type III secretion system effector;
24-271 7.45e-07

type III secretion system effector;


Pssm-ID: 185279  Cd Length: 408  Bit Score: 49.66  E-value: 7.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399   24 RPRDFRCG---RLIVFGDSLSDDGVEAEGESHGFL---------RNCNGKVWPEYVNA-MLECDRYVNYAYSGAKSGPG- 89
Cdd:PRK15381 133 KPKNISLGditRLVFFGDSLSDSLGRMFEKTHHILpsygqyfggRFTNGFTWTEFLSSpHFLGKEMLNFAEGGSTSASYs 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399   90 --NFYFDSFSGIQWQINQFLSNNKFLSddpLVILqtgGTIDFFGGDTNSTEVVenIQQTIQNITQTMSTG--TLVILSLL 165
Cdd:PRK15381 213 cfNCIGDFVSNTDRQVASYTPSHQDLA---IFLL---GANDYMTLHKDNVIMV--VEQQIDDIEKIISGGvnNVLVMGIP 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  166 DVSNSP-GVQAAEDSDILQERLGHliaetNRQLHHIV--LDSDLGTRRLNPFLRVRLIDINTvALAAMQSLNTTEPFTHH 242
Cdd:PRK15381 285 DLSLTPyGKHSDEKRKLKDESIAH-----NALLKTNVeeLKEKYPQHKICYYETADAFKVIM-EAASNIGYDTENPYTHH 358
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 17534399  243 SPDLIPQA-------IYKYAYHDLWNPSTIVHYHIA 271
Cdd:PRK15381 359 GYVHVPGAkdpqldiCPQYVFNDLVHPTQEVHHCFA 394
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
33-197 1.31e-05

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 45.26  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399    33 LIVFGDSLSDDGveaeGEShGFLRNCNGKVWPEYVNAMLE-----CDRYVNYAYSGAKSGpgnfyfDSFSGIQwQINQFL 107
Cdd:pfam00657   1 IVAFGDSLTDGG----GDG-PGGRFSWGDLLADFLARKLGvpgsgYNHGANFAIGGATIE------DLPIQLE-QLLRLI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399   108 SNNKfLSDDPLVILQTGGTIDFFGGDTNSTEVVENIQQTIQNITQTM-----STGTLVILSLLDVSNSPGVQAAE----D 178
Cdd:pfam00657  69 SDVK-DQAKPDLVTIFIGANDLCNFLSSPARSKKRVPDLLDELRANLpqlglGARKFWVHGLGPLGCTPPKGCYElynaL 147
                         170
                  ....*....|....*....
gi 17534399   179 SDILQERLGHLIAETNRQL 197
Cdd:pfam00657 148 AEEYNERLNELVNSLAAAA 166
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
35-203 5.03e-05

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: 42.92  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399    35 VFGDSLSDdGVEAEGESHGFLRncngkVWPEYVNAMLECDRYVNYAYSGAKSGPG-NFYFDSFSGIQWQinqflsnnkfl 113
Cdd:pfam13472   1 ALGDSITA-GYGATGGDRSYPG-----WLARLLARRLGADVVNNLGISGATTRLDlLERLDDVLRLKPD----------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399   114 sddpLVILqTGGTIDFFGGdTNSTEVVENIQQTIQNITQTMSTGTLVILSLLDVSNSPGVQAAEDSDILQeRLGHLIAET 193
Cdd:pfam13472  64 ----LVVI-LLGTNDLGRG-VSAARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLDERRLNARIA-EYNAAIREV 136
                         170
                  ....*....|
gi 17534399   194 NRQLHHIVLD 203
Cdd:pfam13472 137 AAERGVPYVD 146
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
32-165 7.04e-04

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: 39.63  E-value: 7.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534399  32 RLIVFGDSLSdDGVEAEGEshgflrncngKVWPEYVNAMLECD--RYVNYAYSGAKSgpgnfyfdsfSGIQWQINQFLSN 109
Cdd:COG2755  10 RIVALGDSIT-AGYGASRE----------RGWPALLARRLAAAdvRVVNAGISGATT----------ADLLARLDRDLLA 68
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17534399 110 NKFlsDdpLVILQtGGTIDFFGGDTNS-TEVVENIQQTIQNITQTMSTGTLVILSLL 165
Cdd:COG2755  69 LKP--D--LVVIE-LGTNDLLRGLGVSpEEFRANLEALIDRLRAAGPGARVVLVTPP 120
 
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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