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Conserved domains on  [gi|2111031472|ref|WP_225890059|]
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SGNH/GDSL hydrolase family protein [Indioceanicola profundi]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110748)

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:  15522763|35871440
SCOP:  3001315

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 193-395 1.29e-113

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: 330.36  E-value: 1.29e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 193 TIVTLGDSITDGFAATTDQNNRWPDVLAERLNVNNKGPERAVANAGISGNRVLHDIIGPNALARFDRDVLAQPGAEYVVV 272
Cdd:cd01830     1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 273 LEGINDIGFSE-FLPDQEVNAEDIIAGYRQLIERAHSKGLKIYGATLTPFEGAGYFSEEGEAKRQAVNNWIRTSGAFDAV 351
Cdd:cd01830    81 LEGVNDIGASGtDFAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATRQAVNEWIRTSGAFDAV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2111031472 352 IDFDKVTRDPANPRRLLPAYDSGDNLHPSDAGYEAMANSIDLRL 395
Cdd:cd01830   161 VDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
 
Name Accession Description Interval E-value
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 193-395 1.29e-113

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: 330.36  E-value: 1.29e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 193 TIVTLGDSITDGFAATTDQNNRWPDVLAERLNVNNKGPERAVANAGISGNRVLHDIIGPNALARFDRDVLAQPGAEYVVV 272
Cdd:cd01830     1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 273 LEGINDIGFSE-FLPDQEVNAEDIIAGYRQLIERAHSKGLKIYGATLTPFEGAGYFSEEGEAKRQAVNNWIRTSGAFDAV 351
Cdd:cd01830    81 LEGVNDIGASGtDFAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATRQAVNEWIRTSGAFDAV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2111031472 352 IDFDKVTRDPANPRRLLPAYDSGDNLHPSDAGYEAMANSIDLRL 395
Cdd:cd01830   161 VDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 186-391 3.17e-39

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: 139.01  E-value: 3.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 186 TAEEDAATIVTLGDSITDGFAATTDQnnRWPDVLAERLNVNNkgpeRAVANAGISGNRVLhdiigpNALARFDRDVLAQP 265
Cdd:COG2755     3 AAAGKPLRIVALGDSITAGYGASRER--GWPALLARRLAAAD----VRVVNAGISGATTA------DLLARLDRDLLALK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 266 gAEYVVVLEGINDIgfsefLPDQEVNAEDIIAGYRQLIERAHSKG--LKIYGATLTPFEGAGYfseeGEAKRQAVNNWIR 343
Cdd:COG2755    71 -PDLVVIELGTNDL-----LRGLGVSPEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRPNY----LNERIEAYNAAIR 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2111031472 344 TSGA-FDA-VIDFDKVTRDPANprrlLPAYDSGDNLHPSDAGYEAMANSI 391
Cdd:COG2755   141 ELAAeYGVpLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 197-386 3.28e-29

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: 111.87  E-value: 3.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 197 LGDSITDGFAATtDQNNRWPDVLAERLNvnNKGPERAVANAGISGNRVLHDIigpnaLARFDRDVLAQPgaEYVVVLEGI 276
Cdd:pfam13472   2 LGDSITAGYGAT-GGDRSYPGWLARLLA--RRLGADVVNNLGISGATTRLDL-----LERLDDVLRLKP--DLVVILLGT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 277 NDIGFseflpdqEVNAEDIIAGYRQLIERAHSKG--LKIYGA-TLTPFEGAGYFSEEGEAKRQAVNNWIRTSGAFD--AV 351
Cdd:pfam13472  72 NDLGR-------GVSAARAAANLEALIDALRAAGpdARVLLIgPLPVGPPPPLDERRLNARIAEYNAAIREVAAERgvPY 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2111031472 352 IDFDKVTRDPANPrrlLPAYDSGDNLHPSDAGYEA 386
Cdd:pfam13472 145 VDLWDALRDDGGW---LPDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 193-395 1.29e-113

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: 330.36  E-value: 1.29e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 193 TIVTLGDSITDGFAATTDQNNRWPDVLAERLNVNNKGPERAVANAGISGNRVLHDIIGPNALARFDRDVLAQPGAEYVVV 272
Cdd:cd01830     1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 273 LEGINDIGFSE-FLPDQEVNAEDIIAGYRQLIERAHSKGLKIYGATLTPFEGAGYFSEEGEAKRQAVNNWIRTSGAFDAV 351
Cdd:cd01830    81 LEGVNDIGASGtDFAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATRQAVNEWIRTSGAFDAV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2111031472 352 IDFDKVTRDPANPRRLLPAYDSGDNLHPSDAGYEAMANSIDLRL 395
Cdd:cd01830   161 VDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 186-391 3.17e-39

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: 139.01  E-value: 3.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 186 TAEEDAATIVTLGDSITDGFAATTDQnnRWPDVLAERLNVNNkgpeRAVANAGISGNRVLhdiigpNALARFDRDVLAQP 265
Cdd:COG2755     3 AAAGKPLRIVALGDSITAGYGASRER--GWPALLARRLAAAD----VRVVNAGISGATTA------DLLARLDRDLLALK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 266 gAEYVVVLEGINDIgfsefLPDQEVNAEDIIAGYRQLIERAHSKG--LKIYGATLTPFEGAGYfseeGEAKRQAVNNWIR 343
Cdd:COG2755    71 -PDLVVIELGTNDL-----LRGLGVSPEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRPNY----LNERIEAYNAAIR 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2111031472 344 TSGA-FDA-VIDFDKVTRDPANprrlLPAYDSGDNLHPSDAGYEAMANSI 391
Cdd:COG2755   141 ELAAeYGVpLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 197-386 3.28e-29

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: 111.87  E-value: 3.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 197 LGDSITDGFAATtDQNNRWPDVLAERLNvnNKGPERAVANAGISGNRVLHDIigpnaLARFDRDVLAQPgaEYVVVLEGI 276
Cdd:pfam13472   2 LGDSITAGYGAT-GGDRSYPGWLARLLA--RRLGADVVNNLGISGATTRLDL-----LERLDDVLRLKP--DLVVILLGT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 277 NDIGFseflpdqEVNAEDIIAGYRQLIERAHSKG--LKIYGA-TLTPFEGAGYFSEEGEAKRQAVNNWIRTSGAFD--AV 351
Cdd:pfam13472  72 NDLGR-------GVSAARAAANLEALIDALRAAGpdARVLLIgPLPVGPPPPLDERRLNARIAEYNAAIREVAAERgvPY 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2111031472 352 IDFDKVTRDPANPrrlLPAYDSGDNLHPSDAGYEA 386
Cdd:pfam13472 145 VDLWDALRDDGGW---LPDLLADDGLHPNAAGYRL 176
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
194-391 5.43e-27

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 106.89  E-value: 5.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 194 IVTLGDSITDGFAATTDQNNRWPDVLAERLNvNNKGPE----RAVANAGISGNRVLHDIIGPNALARFDRDVLAQPGAEY 269
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGGRFSWGDLLADFLA-RKLGVPgsgyNHGANFAIGGATIEDLPIQLEQLLRLISDVKDQAKPDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 270 VVVLEGINDIGFSEFLPDQ-----EVNAEDIIAGYRQL---IERAHSKGLKIYGATLtPFEGAGYFSEEGEAKRQAVNNW 341
Cdd:pfam00657  80 VTIFIGANDLCNFLSSPARskkrvPDLLDELRANLPQLglgARKFWVHGLGPLGCTP-PKGCYELYNALAEEYNERLNEL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2111031472 342 IRTSGAF---DAVIDFDkvTRDPANPRRLLPAYDSG-DNLHPSDAGYEAMANSI 391
Cdd:pfam00657 159 VNSLAAAaedANVVYVD--IYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 194-389 4.66e-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: 84.30  E-value: 4.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 194 IVTLGDSITDGFAATTDqnNRWPDVLAERLNVNnkgperaVANAGISGNRVlhdiigPNALARFDRDVLA-QPGaeYVVV 272
Cdd:cd04501     3 VVCLGDSITYGYPVGPE--ASWVNLLAEFLGKE-------VINRGINGDTT------SQMLVRFYEDVIAlKPA--VVII 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 273 LEGINDIGfseflpdQEVNAEDIIAGYRQLIERAHSKGLKIYGATLTPF--EGAGYFSEEGEAKRQAVNNWI----RTSG 346
Cdd:cd04501    66 MGGTNDII-------VNTSLEMIKDNIRSMVELAEANGIKVILASPLPVddYPWKPQWLRPANKLKSLNRWLkdyaRENG 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2111031472 347 AFdaVIDFDKVTRDPANpRRLLPAYdSGDNLHPSDAGYEAMAN 389
Cdd:cd04501   139 LL--FLDFYSPLLDERN-VGLKPGL-LTDGLHPSREGYRVMAP 177
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 194-391 4.74e-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: 75.91  E-value: 4.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 194 IVTLGDSITDGFAATTDQNNRWPDVlaeRLNVNNKGPERAVANAGISGNRVLHDIIGpnalaRFDRDVLAQPGAEYVVVL 273
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLL---YLLLLAGGPGVEVINLGVSGATTADALRR-----LGLRLALLKDKPDLVIIE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 274 EGINDIGFseflpDQEVNAEDIIAGYRQLIERAH--SKGLKIYGATLTPFEGAGYFSEEGEAKR----QAVNNWIRtSGA 347
Cdd:cd00229    73 LGTNDLGR-----GGDTSIDEFKANLEELLDALRerAPGAKVILITPPPPPPREGLLGRALPRYneaiKAVAAENP-APS 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2111031472 348 FDAVIDFDKVTRDPANPrrllpaYDSGDNLHPSDAGYEAMANSI 391
Cdd:cd00229   147 GVDLVDLAALLGDEDKS------LYSPDGIHPNPAGHKLIAEAL 184
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 194-392 3.16e-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: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 194 IVTLGDSITDG-----FAATtdqnnrwpdVLAERLnvnnkgPERAVA--NAGISGNRVLHdiigpnALARFDRDVLAQPg 266
Cdd:cd01834     4 IVFIGNSITDRggyvgYVET---------YLAARY------PELKLTfrNLGWSGDTVSD------LAARRDRDVLPAK- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 267 AEYVVVLEGINDIGFsefLPDQEVNAEDIIAGYRQLIERAHSK--GLKIYGATLTPFEGAGY---FSEEGEAKRQAVNNW 341
Cdd:cd01834    62 PDVVSIMFGINDSFR---GFDDPVGLEKFKTNLRRLIDRLKNKesAPRIVLVSPIAYEANEDplpDGAEYNANLAAYADA 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2111031472 342 IRTSGAFD--AVIDFDKVTRDpaNPRRLLPAYDSGDNLHPSDAGYEAMANSID 392
Cdd:cd01834   139 VRELAAENgvAFVDLFTPMKE--AFQKAGEAVLTVDGVHPNEAGHRALARLWL 189
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 197-389 1.16e-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: 68.03  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 197 LGDSITDGfaattDQNNrwpdvlaerlnvnnkgperavanAGISGNrvLHDIIgpnalARFDRDVLAQPGAEYVVVLEGI 276
Cdd:cd01833     6 LGDSITWG-----DKDH-----------------------EGHSGY--LIDQI-----AAAAADWVLAAKPDVVLLHLGT 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 277 NDIgfseflpDQEVNAEDIIAGYRQLIE--RAHSKGLKIYGATLTPFEGAGyfseeGEAKRQAVNNWI-------RTSGA 347
Cdd:cd01833    51 NDL-------VLNRDPDTAPDRLRALIDqmRAANPDVKIIVATLIPTTDAS-----GNARIAEYNAAIpgvvadlRTAGS 118

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2111031472 348 FDAVIDFdkvtrdpanPRRLLPAYDSGDNLHPSDAGYEAMAN 389
Cdd:cd01833   119 PVVLVDM---------STGYTTADDLYDGLHPNDQGYKKMAD 151
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 192-391 1.82e-13

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: 68.31  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 192 ATIVTLGDSITDGFAATTDQNnrWPDVLAERLnvNNKGPERAVANAGISGnrvlhDIIGpNALARFDRdVLAQPGAEYVV 271
Cdd:cd01822     1 VTILALGDSLTAGYGLPPEEG--WPALLQKRL--DARGIDVTVINAGVSG-----DTTA-GGLARLPA-LLAQHKPDLVI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 272 VLEGINDI--GFSeflPDQevnaedIIAGYRQLIERAHSKGLKIY--GATLTPFEGAGYFseegeakRQAVNNWIRTSGA 347
Cdd:cd01822    70 LELGGNDGlrGIP---PDQ------TRANLRQMIETAQARGAPVLlvGMQAPPNYGPRYT-------RRFAAIYPELAEE 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2111031472 348 FDAVID---FDKVTRDPAnprrLLpaydSGDNLHPSDAGYEAMANSI 391
Cdd:cd01822   134 YGVPLVpffLEGVAGDPE----LM----QSDGIHPNAEGQPIIAENV 172
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 194-391 4.93e-13

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: 66.53  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 194 IVTLGDSITDGFaattdqnnRWPDVLaerlnvnnkgPERAVANAGISGNRVlhdiIGpnALARFDRDVLAQPGAeyVVVL 273
Cdd:cd01828     2 LVFLGDSLTEGG--------PWALLF----------PDVKVANRGISGDTT----RG--LLARLDEDVALQPKA--IFIM 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 274 EGINDIGfseflpdQEVNAEDIIAGYRQLIE--RAHSKGLKIYGATLTPFEGAGYFSEEgeaKRQAVNNWI----RTSGA 347
Cdd:cd01828    56 IGINDLA-------QGTSDEDIVANYRTILEklRKHFPNIKIVVQSILPVGELKSIPNE---QIEELNRQLaqlaQQEGV 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2111031472 348 fdAVIDFDKVTrdpANPRRLLPAYDSGDNLHPSDAGYEAMANSI 391
Cdd:cd01828   126 --TFLDLWAVF---TNADGDLKNEFTTDGLHLNAKGYAVWAAAL 164
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 193-391 1.66e-08

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: 53.87  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 193 TIVTLGDSITDGfaattdqnnrWPDVlaerlNVNNKGPEraVANAGISG--NRVLHDIIGPNalarfdrdvLAQPGAEYV 270
Cdd:cd01841     2 NIVFIGDSLFEG----------WPLY-----EAEGKGKT--VNNLGIAGisSRQYLEHIEPQ---------LIQKNPSKV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 271 VVLEGINDIGFseflpdqEVNAEDIIAGYRQLIE--RAHSKGLKIYGATLTPFEGAGYFSEEGEAKRQAVNNWIRTSGAF 348
Cdd:cd01841    56 FLFLGTNDIGK-------EVSSNQFIKWYRDIIEqiREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIQRLNDAIKELAPE 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2111031472 349 DAV--IDFDKVTRDPANPrrlLPAYDSGDNLHPSDAGYEAMANSI 391
Cdd:cd01841   129 LGVtfIDLNDVLVDEFGN---LKKEYTTDGLHFNPKGYQKLLEIL 170
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 194-388 8.72e-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: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 194 IVTLGDSITDGFAATTDQN--NRWPDVLAERLNVNNkgPERAVANAGISGnRVLHDIIG---PNALARfdrdvlaqpGAE 268
Cdd:cd01832     2 YVALGDSITEGVGDPVPDGgyRGWADRLAAALAAAD--PGIEYANLAVRG-RRTAQILAeqlPAALAL---------RPD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 269 YVVVLEGINDIgfseFLPDqeVNAEDIIAGYRQLIERAHSKGLKIYGATLTPFEGAGYFSEEGEAKRQAVNNWIRT-SGA 347
Cdd:cd01832    70 LVTLLAGGNDI----LRPG--TDPDTYRADLEEAVRRLRAAGARVVVFTIPDPAVLEPFRRRVRARLAAYNAVIRAvAAR 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2111031472 348 FDAV-IDFDkvtrdpANPRRLLPAYDSGDNLHPSDAGYEAMA 388
Cdd:cd01832   144 YGAVhVDLW------EHPEFADPRLWASDRLHPSAAGHARLA 179
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 193-391 5.05e-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. This subfamily contains sequences similar to Bacillus YpmR.


Pssm-ID: 239947  Cd Length: 204  Bit Score: 49.94  E-value: 5.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 193 TIVTLGDSITDGfaaTTDQNNR--WPDVLAERLNVNNKGPERaVANAGISGNRVlhdiigPNALARFD----RDVLAQpg 266
Cdd:cd04506     1 KIVALGDSLTEG---VGDETGKggYVGRLDKLIETKTVKKVT-VQNFGVSGDRS------DQLLKRLKtkkvQKELKK-- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 267 AEYVVVLEGIND---IGFSEFLPDQEVNAEDIIAGYRQ-------LIERAHSKG----LKIYgatlTPFEGagYFSEEGE 332
Cdd:cd04506    69 ADVITITIGGNDlmqVLEKNFLSLDVEDFKKAEETYQNnlkkifkEIRKLNPDApiflVGLY----NPFYV--YFPNITE 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2111031472 333 AKrQAVNNWIRTSGA----FDAV--IDFDKVTRDPANPRrllpaYDSGDNLHPSDAGYEAMANSI 391
Cdd:cd04506   143 IN-DIVNDWNEASQKlasqYKNAyfVPIFDLFSDGQNKY-----LLTSDHFHPNDKGYQLIADRV 201
Endoglucanase_E_like cd01831
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
 198-391 9.40e-05

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: 42.72  E-value: 9.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 198 GDSITDGF-----------AATTDQNNRWPDVLAERLNVNNkgpeRAVANAGIsgnrvlhdiigpnalarfdrdvlaqpG 266
Cdd:cd01831     6 GDSITCGYgvtgksrcdfsAATEDPSLSYAALLARALNAEY----SIIAYSGI--------------------------G 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 267 AEYVVVLEGINDigfseFLPDQEVNAEDIIAGYRQLIERAHskglKIYG-----ATLTPFeGAGYFSEEGEAKRQAVNNw 341
Cdd:cd01831    56 PDLVVINLGTND-----FSTGNNPPGEDFTNAYVEFIEELR----KRYPdapivLMLGPM-LFGPYGTEEEIKRVAEAF- 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2111031472 342 IRTSGAFDAVIDFDkvtrdpanprRLLPAYDSGDNLHPSDAGYEAMANSI 391
Cdd:cd01831   125 KDQKSKKVHYFDTP----------GILQHNDIGCDWHPTVAGHQKIAKHL 164
fatty_acyltransferase_like cd01846
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ...
 193-312 4.70e-04

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: 41.60  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 193 TIVTLGDSITD---GFAATTD---------QNNR------WPDVLAERLNVNNKGPER--AVANAGISGNRVLHDIIGPN 252
Cdd:cd01846     1 RLVVFGDSLSDtgnIFKLTGGsnpppsppyFGGRfsngpvWVEYLAATLGLSGLKQGYnyAVGGATAGAYNVPPYPPTLP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2111031472 253 ALAR----FDRDVLAQPGAEYVVVLE-GINDIGFSEFLP-DQEVNAEDIIAGYRQLIERAHSKGLK 312
Cdd:cd01846    81 GLSDqvaaFLAAHKLRLPPDTLVAIWiGANDLLNALDLPqNPDTLVTRAVDNLFQALQRLYAAGAR 146
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
 193-304 1.16e-03

SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating enzyme) of A. tumefaciens. 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: 238877  Cd Length: 208  Bit Score: 39.94  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111031472 193 TIVTLGDSITDGFAATT----DQNNRWPDVLAERLnvNNKGPERAVANAGISGNR-VLHDIIGP--NALARFDRDVLAQP 265
Cdd:cd01839     1 TILCFGDSNTWGIIPDTggryPFEDRWPGVLEKAL--GANGENVRVIEDGLPGRTtVLDDPFFPgrNGLTYLPQALESHS 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2111031472 266 GAEYVVVLEGINDIgFSEFlpdqEVNAEDIIAGYRQLIE 304
Cdd:cd01839    79 PLDLVIIMLGTNDL-KSYF----NLSAAEIAQGLGALVD 112
 
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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