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Conserved domains on  [gi|1442588620|gb|RDS80354|]
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SGNH/GDSL hydrolase family protein [Dyella psychrodurans]

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 ...
194-400 3.00e-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: 324.58  E-value: 3.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 194 AVVAFGDSITDGIMSTPNANHRWPDVFAERLQADPKLSSIAVVNSGISGNRILHDGGGPSALSRFDRDALDKPGVHWIVL 273
Cdd:cd01830     1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 274 LEGINDIGASGQPsTPEDNVSAQQIIDGMKTLISKAHAKGIKIFGATLTPFGgaGWPYHTAAGEEKRQAVNAWIRTSGAF 353
Cdd:cd01830    81 LEGVNDIGASGTD-FAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFE--GSGYYTPAREATRQAVNEWIRTSGAF 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1442588620 354 DAVIDFDKVVRDPAHPDRFLPEFDSGDHLHPGDAGYRAMADSIDLSL 400
Cdd:cd01830   158 DAVVDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
 
Name Accession Description Interval E-value
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
194-400 3.00e-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: 324.58  E-value: 3.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 194 AVVAFGDSITDGIMSTPNANHRWPDVFAERLQADPKLSSIAVVNSGISGNRILHDGGGPSALSRFDRDALDKPGVHWIVL 273
Cdd:cd01830     1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 274 LEGINDIGASGQPsTPEDNVSAQQIIDGMKTLISKAHAKGIKIFGATLTPFGgaGWPYHTAAGEEKRQAVNAWIRTSGAF 353
Cdd:cd01830    81 LEGVNDIGASGTD-FAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFE--GSGYYTPAREATRQAVNEWIRTSGAF 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1442588620 354 DAVIDFDKVVRDPAHPDRFLPEFDSGDHLHPGDAGYRAMADSIDLSL 400
Cdd:cd01830   158 DAVVDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
188-396 6.79e-37

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: 132.85  E-value: 6.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 188 AGESARAVVAFGDSITDGIMSTPNanHRWPDVFAERLQADPklssIAVVNSGISGNRILHdgggpsALSRFDRDALDKPg 267
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYGASRE--RGWPALLARRLAAAD----VRVVNAGISGATTAD------LLARLDRDLLALK- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 268 VHWIVLLEGINDIGASgqpstpeDNVSAQQIIDGMKTLISKAHAKG--IKIFGATLTPFGGAGwpyhtaAGEEKRQAVNA 345
Cdd:COG2755    71 PDLVVIELGTNDLLRG-------LGVSPEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRPN------YLNERIEAYNA 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1442588620 346 WIRTSGA-FDA-VIDFDKVVRDPAHpdrfLPEFDSGDHLHPGDAGYRAMADSI 396
Cdd:COG2755   138 AIRELAAeYGVpLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
197-391 4.74e-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: 111.48  E-value: 4.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 197 AFGDSITDGiMSTPNANHRWPDVFAERLQAdpKLSSIAVVNSGISGNRILHDgggpsALSRFDRDALDKPgvHWIVLLEG 276
Cdd:pfam13472   1 ALGDSITAG-YGATGGDRSYPGWLARLLAR--RLGADVVNNLGISGATTRLD-----LLERLDDVLRLKP--DLVVILLG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 277 INDIGASGQPSTPEDNVsaQQIIDGMKtliskAHAKGIKIFGATLTPFGGAGWPYhTAAGEEKRQAVNAWIRTSGAFD-- 354
Cdd:pfam13472  71 TNDLGRGVSAARAAANL--EALIDALR-----AAGPDARVLLIGPLPVGPPPPLD-ERRLNARIAEYNAAIREVAAERgv 142
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1442588620 355 AVIDFDKVVRDPAHPdrfLPEFDSGDHLHPGDAGYRA 391
Cdd:pfam13472 143 PYVDLWDALRDDGGW---LPDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
194-400 3.00e-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: 324.58  E-value: 3.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 194 AVVAFGDSITDGIMSTPNANHRWPDVFAERLQADPKLSSIAVVNSGISGNRILHDGGGPSALSRFDRDALDKPGVHWIVL 273
Cdd:cd01830     1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 274 LEGINDIGASGQPsTPEDNVSAQQIIDGMKTLISKAHAKGIKIFGATLTPFGgaGWPYHTAAGEEKRQAVNAWIRTSGAF 353
Cdd:cd01830    81 LEGVNDIGASGTD-FAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFE--GSGYYTPAREATRQAVNEWIRTSGAF 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1442588620 354 DAVIDFDKVVRDPAHPDRFLPEFDSGDHLHPGDAGYRAMADSIDLSL 400
Cdd:cd01830   158 DAVVDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
188-396 6.79e-37

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: 132.85  E-value: 6.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 188 AGESARAVVAFGDSITDGIMSTPNanHRWPDVFAERLQADPklssIAVVNSGISGNRILHdgggpsALSRFDRDALDKPg 267
Cdd:COG2755     4 AAGKPLRIVALGDSITAGYGASRE--RGWPALLARRLAAAD----VRVVNAGISGATTAD------LLARLDRDLLALK- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 268 VHWIVLLEGINDIGASgqpstpeDNVSAQQIIDGMKTLISKAHAKG--IKIFGATLTPFGGAGwpyhtaAGEEKRQAVNA 345
Cdd:COG2755    71 PDLVVIELGTNDLLRG-------LGVSPEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRPN------YLNERIEAYNA 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1442588620 346 WIRTSGA-FDA-VIDFDKVVRDPAHpdrfLPEFDSGDHLHPGDAGYRAMADSI 396
Cdd:COG2755   138 AIRELAAeYGVpLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
197-391 4.74e-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: 111.48  E-value: 4.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 197 AFGDSITDGiMSTPNANHRWPDVFAERLQAdpKLSSIAVVNSGISGNRILHDgggpsALSRFDRDALDKPgvHWIVLLEG 276
Cdd:pfam13472   1 ALGDSITAG-YGATGGDRSYPGWLARLLAR--RLGADVVNNLGISGATTRLD-----LLERLDDVLRLKP--DLVVILLG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 277 INDIGASGQPSTPEDNVsaQQIIDGMKtliskAHAKGIKIFGATLTPFGGAGWPYhTAAGEEKRQAVNAWIRTSGAFD-- 354
Cdd:pfam13472  71 TNDLGRGVSAARAAANL--EALIDALR-----AAGPDARVLLIGPLPVGPPPPLD-ERRLNARIAEYNAAIREVAAERgv 142
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1442588620 355 AVIDFDKVVRDPAHPdrfLPEFDSGDHLHPGDAGYRA 391
Cdd:pfam13472 143 PYVDLWDALRDDGGW---LPDLLADDGLHPNAAGYRL 176
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
195-396 4.54e-24

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 98.80  E-value: 4.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITDGIMSTPNANHRWPDVFAERLQAD---PKLSSIAVVNSGISGNRILHDGGGPSALSRFDRDALDKPGVHWI 271
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGGRFSWGDLLADFLARKlgvPGSGYNHGANFAIGGATIEDLPIQLEQLLRLISDVKDQAKPDLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 272 VLLEGINDI---GASGQPSTPEDNVSAQQIIDGMKTL---ISKAHAKGIKIFGAtlTPFGGAGWPYHtAAGEEKRQAVNA 345
Cdd:pfam00657  81 TIFIGANDLcnfLSSPARSKKRVPDLLDELRANLPQLglgARKFWVHGLGPLGC--TPPKGCYELYN-ALAEEYNERLNE 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1442588620 346 WIRTSGAF---DAVIDFDkvVRDPAHPDRFLPEFDSG-DHLHPGDAGYRAMADSI 396
Cdd:pfam00657 158 LVNSLAAAaedANVVYVD--IYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
195-400 6.42e-18

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: 80.83  E-value: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITDGIMSTPNANhrWPDVFAErlqadpkLSSIAVVNSGISGNRIlhdgggPSALSRFDRDALD-KPGVhwIVL 273
Cdd:cd04501     3 VVCLGDSITYGYPVGPEAS--WVNLLAE-------FLGKEVINRGINGDTT------SQMLVRFYEDVIAlKPAV--VII 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 274 LEGINDIGAsgqpstpedNVSAQQIIDGMKTLISKAHAKGIKIFGATLTPFGGAGWPYHTAAGEEKRQAVNAWI----RT 349
Cdd:cd04501    66 MGGTNDIIV---------NTSLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWLRPANKLKSLNRWLkdyaRE 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1442588620 350 SGAFdaVIDFDKVVRDPAHpdRFLPEFDSGDHLHPGDAGYRAMADSIDLSL 400
Cdd:cd04501   137 NGLL--FLDFYSPLLDERN--VGLKPGLLTDGLHPSREGYRVMAPLAEKAL 183
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
195-396 1.24e-17

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: 80.15  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITDGIMSTPNANHRWPDVfaeRLQADPKLSSIAVVNSGISGNRILHdggGPSALSRFDRDALDKPGvhWIVLL 274
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLL---YLLLLAGGPGVEVINLGVSGATTAD---ALRRLGLRLALLKDKPD--LVIIE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 275 EGINDIGASGqpstpedNVSAQQIIDGMKTLISKAH--AKGIKIFGATLTPFGGAGWPYHTAAGE--EKRQAVNAWIRtS 350
Cdd:cd00229    73 LGTNDLGRGG-------DTSIDEFKANLEELLDALRerAPGAKVILITPPPPPPREGLLGRALPRynEAIKAVAAENP-A 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1442588620 351 GAFDAVIDFDKVVRDPahpdrfLPEFDSGDHLHPGDAGYRAMADSI 396
Cdd:cd00229   145 PSGVDLVDLAALLGDE------DKSLYSPDGIHPNPAGHKLIAEAL 184
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
195-397 6.70e-15

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: 72.71  E-value: 6.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAF-GDSITDGIMstpnanhrWPDVFAERLQA-DPKLSsIAVVNSGISGNRILHdgggpsALSRFDRDALD-KPgvHWI 271
Cdd:cd01834     3 RIVFiGNSITDRGG--------YVGYVETYLAArYPELK-LTFRNLGWSGDTVSD------LAARRDRDVLPaKP--DVV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 272 VLLEGINDIGAsgqpsTPEDNVSAQQIIDGMKTLI----SKAHAKGIkifgATLTPF---GGAGWPYHTAAGEEKRQAVN 344
Cdd:cd01834    66 SIMFGINDSFR-----GFDDPVGLEKFKTNLRRLIdrlkNKESAPRI----VLVSPIayeANEDPLPDGAEYNANLAAYA 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1442588620 345 AWIRTSGAFD--AVIDFDKVVRDpaHPDRFLPEFDSGDHLHPGDAGYRAMADSID 397
Cdd:cd01834   137 DAVRELAAENgvAFVDLFTPMKE--AFQKAGEAVLTVDGVHPNEAGHRALARLWL 189
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
195-396 4.47e-10

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: 58.29  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITDGimSTPNANHRWPDVFAERLQAdpKLSSIAVVNSGISGnrilhD--GGGpsaLSRFDRdALDKPGVHWIV 272
Cdd:cd01822     3 ILALGDSLTAG--YGLPPEEGWPALLQKRLDA--RGIDVTVINAGVSG-----DttAGG---LARLPA-LLAQHKPDLVI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 273 LLEGINDiGASGQPstpednvsAQQIIDGMKTLISKAHAKGIKIFgatLtpfggAGWPYHTAAGEEKRQAVNA-WIRTSG 351
Cdd:cd01822    70 LELGGND-GLRGIP--------PDQTRANLRQMIETAQARGAPVL---L-----VGMQAPPNYGPRYTRRFAAiYPELAE 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1442588620 352 AFDAVID---FDKVVRDpahpdrflPEFDSGDHLHPGDAGYRAMADSI 396
Cdd:cd01822   133 EYGVPLVpffLEGVAGD--------PELMQSDGIHPNAEGQPIIAENV 172
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
194-396 9.35e-09

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: 9.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 194 AVVAFGDSITDGimstpnanHRWPDVFaerlqadpklSSIAVVNSGISGNRIlhDGggpsALSRFDRDALDKPgvHWIVL 273
Cdd:cd01828     1 ALVFLGDSLTEG--------GPWALLF----------PDVKVANRGISGDTT--RG----LLARLDEDVALQP--KAIFI 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 274 LEGINDIGAsgqpstpedNVSAQQIIDGMKTLISKA--HAKGIKIFGATLTPFGGAGWpyHTAageEKRQAVN----AWI 347
Cdd:cd01828    55 MIGINDLAQ---------GTSDEDIVANYRTILEKLrkHFPNIKIVVQSILPVGELKS--IPN---EQIEELNrqlaQLA 120
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1442588620 348 RTSGAfdAVIDFDKVVRDpahPDRFLPEFDSGDHLHPGDAGYRAMADSI 396
Cdd:cd01828   121 QQEGV--TFLDLWAVFTN---ADGDLKNEFTTDGLHLNAKGYAVWAAAL 164
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
271-394 2.70e-08

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: 52.62  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 271 IVLLE-GINDIGAsgqpstpedNVSAQQIIDGMKTLISK--AHAKGIKIFGATLTPfggagwpYHTAAGEEKRQAVNAWI 347
Cdd:cd01833    43 VVLLHlGTNDLVL---------NRDPDTAPDRLRALIDQmrAANPDVKIIVATLIP-------TTDASGNARIAEYNAAI 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1442588620 348 RtSGAFDAVIDFDKVVRDPAHPDrFLPEFDSGDHLHPGDAGYRAMAD 394
Cdd:cd01833   107 P-GVVADLRTAGSPVVLVDMSTG-YTTADDLYDGLHPNDQGYKKMAD 151
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
195-396 4.63e-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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


Pssm-ID: 238870  Cd Length: 185  Bit Score: 46.88  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITDGIMSTPNANH--RWPDVFAERLqaDPKLSSIAVVNSGISGNRILHDGGG---PSALSRFDRdaldkpgvh 269
Cdd:cd01832     2 YVALGDSITEGVGDPVPDGGyrGWADRLAAAL--AAADPGIEYANLAVRGRRTAQILAEqlpAALALRPDL--------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 270 wIVLLEGINDIgasGQPSTPEDNVSAqQIIDGMKTLIskAHakgikifGATLTPFGGAGWPYHTAAGEEKRQ---AVNAW 346
Cdd:cd01832    71 -VTLLAGGNDI---LRPGTDPDTYRA-DLEEAVRRLR--AA-------GARVVVFTIPDPAVLEPFRRRVRArlaAYNAV 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1442588620 347 IRT-SGAFDAVidfdkVVRDPAHPDRFLPEFDSGDHLHPGDAGYRAMADSI 396
Cdd:cd01832   137 IRAvAARYGAV-----HVDLWEHPEFADPRLWASDRLHPSAAGHARLAALV 182
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
195-394 8.00e-06

PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction.


Pssm-ID: 238858  Cd Length: 214  Bit Score: 46.51  E-value: 8.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITDGIMSTPNANhrWPDVFAERlqadpklssiAVVNSGISGNRILHdgggpsALSRFDRDALDkpGVH--WIV 272
Cdd:cd01820    35 VVFIGDSITQNWEFTGLEV--WRELYAPL----------HALNFGIGGDRTQN------VLWRLENGELD--GVNpkVVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 273 LLEGINDIGASGqpstpednvSAQQIIDGMKTLISKAHAK--GIKIFGATLTPFGgagwpYHTAAGEEKRQAVNAWIRts 350
Cdd:cd01820    95 LLIGTNNIGHTT---------TAEEIAEGILAIVEEIREKlpNAKILLLGLLPRG-----QNPNPLRERNAQVNRLLA-- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1442588620 351 GAFDAVIDFDKVVRDPAHPDRF--LPEFDSGDHLHPGDAGYRAMAD 394
Cdd:cd01820   159 VRYDGLPNVTFLDIDKGFVQSDgtISHHDMPDYLHLTAAGYRKWAD 204
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
195-306 5.51e-04

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: 41.10  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITDGI--MSTP--NANHRWPDVFAERLQADpkLSSIAVVNSGISGNRILHDggGPSALSRFDRDALD------ 264
Cdd:cd01839     2 ILCFGDSNTWGIipDTGGryPFEDRWPGVLEKALGAN--GENVRVIEDGLPGRTTVLD--DPFFPGRNGLTYLPqalesh 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1442588620 265 KPGVHWIVLLeGINDIgasgqpsTPEDNVSAQQIIDGMKTLI 306
Cdd:cd01839    78 SPLDLVIIML-GTNDL-------KSYFNLSAAEIAQGLGALV 111
fatty_acyltransferase_like cd01846
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ...
195-394 1.19e-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: 40.44  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITD--GIM----------STPNANHR------WPDVFAERLQADPKLSSI--AVVNSGISGNRILHDGGGPSA 254
Cdd:cd01846     2 LVVFGDSLSDtgNIFkltggsnpppSPPYFGGRfsngpvWVEYLAATLGLSGLKQGYnyAVGGATAGAYNVPPYPPTLPG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 255 LS------------RFDRDALdkpGVHWIvlleGINDIGASGQPSTPEDNvSAQQIIDGMKTLISKAHAKGIK---IFG- 318
Cdd:cd01846    82 LSdqvaaflaahklRLPPDTL---VAIWI----GANDLLNALDLPQNPDT-LVTRAVDNLFQALQRLYAAGARnflVLNl 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 319 --ATLTPFGGAGWPYHTAAGEEKRQAVNAWIRT-SGAFDA--------VID----FDKVVRDPA------HPDRFLPEFD 377
Cdd:cd01846   154 pdLGLTPAFQAQGDAVAARATALTAAYNAKLAEkLAELKAqhpgvnilLFDtnalFNDILDNPAaygftnVTDPCLDYVY 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1442588620 378 SG---------------DHLHPGDAGYRAMAD 394
Cdd:cd01846   234 SYspreacanpdkylfwDEVHPTTAVHQLIAE 265
COG3240 COG3240
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function ...
195-396 5.99e-03

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


Pssm-ID: 442472 [Multi-domain]  Cd Length: 305  Bit Score: 38.48  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 195 VVAFGDSITD----------GIMSTPNANHR------WPDVFAERLQADPKLSSIAVVNSGISGNRIlHDGGGPSALS-- 256
Cdd:COG3240    31 IVVFGDSLSDtgnlfnltggLPPSPPYFGGRfsngpvWVEYLAAALGLPLTPSSAGGTNYAVGGART-GDGNGVLGGAal 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 257 -----------------RFDRDALdkpGVHWIvlleGINDI-----GASGQPSTPEDNV--SAQQIIDGMKTLIsKAHAK 312
Cdd:COG3240   110 lpglaqqvdaylaaaggTADPNAL---YIVWA----GANDLlaalaAVGATPAQAQAAAtaAAANLAAAVGALA-AAGAR 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442588620 313 GIKIFGA---TLTPFGGAGWPYHTAAGEEKRQAVNAWIRT----SGA----FDAVIDFDKVVRDP--------------- 366
Cdd:COG3240   182 HILVPNLpdlGLTPAAQALGAAAAALLSALTAAFNQALAAalpaLGVniilFDVNSLFNEIIANPaaygftnvtdaclsg 261
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1442588620 367 --------AHPDRFLpeFDsgDHLHPGDAGYRAMADSI 396
Cdd:COG3240   262 tvsallcvANPDTYL--FW--DGVHPTTAAHRLIADYA 295
 
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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