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Conserved domains on  [gi|490429420|ref|WP_004301559|]
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MULTISPECIES: SGNH/GDSL hydrolase family protein [Bacteroides]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 85)

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; similar to plant GDSL esterase/lipase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lipase_GDSL_3 super family cl46856
GDSL-like Lipase/Acylhydrolase family;
24-224 8.34e-123

GDSL-like Lipase/Acylhydrolase family;


The actual alignment was detected with superfamily member pfam16255:

Pssm-ID: 481196  Cd Length: 203  Bit Score: 346.70  E-value: 8.34e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420   24 KSISILGDSYSTFEGYLQPDTNSIWYYVSPRQ--QTDVTSVKQTWWHKFIKENNYRLCVNNSFSGATICNTGYNQADYSD 101
Cdd:pfam16255   1 KSVSILGDSYSTFEGYVQPDTNFVWYLKTPPKgrKTDMVSVRNTWWHQFIKENNYRLCVNNSFSGATICHTGYRSEDYSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  102 RSFITRMDKLGCPDIIFIFGATNDCWAGSPLGDYKYEGWTKEDLYTFRPAMAYLLDHMIDRYPNVEIYFLLNSGLKEEFN 181
Cdd:pfam16255  81 RSFITRMKALGCPDIIFIFGATNDYWAKSPLGEYKYADWSKKDLYSFRPAMAYMLDTMIDYYPNVEIYFLLNDGLGNEIT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 490429420  182 ESVRAICNHYNIDCIELHDIDKKSGHPSIKGMEQISEQIKMFM 224
Cdd:pfam16255 161 ESVRTICKHYQIDCIELKELDKMSGHPSVKGMKQISEQVKAYM 203
 
Name Accession Description Interval E-value
Lipase_GDSL_lke pfam16255
GDSL-like Lipase/Acylhydrolase;
24-224 8.34e-123

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 435238  Cd Length: 203  Bit Score: 346.70  E-value: 8.34e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420   24 KSISILGDSYSTFEGYLQPDTNSIWYYVSPRQ--QTDVTSVKQTWWHKFIKENNYRLCVNNSFSGATICNTGYNQADYSD 101
Cdd:pfam16255   1 KSVSILGDSYSTFEGYVQPDTNFVWYLKTPPKgrKTDMVSVRNTWWHQFIKENNYRLCVNNSFSGATICHTGYRSEDYSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  102 RSFITRMDKLGCPDIIFIFGATNDCWAGSPLGDYKYEGWTKEDLYTFRPAMAYLLDHMIDRYPNVEIYFLLNSGLKEEFN 181
Cdd:pfam16255  81 RSFITRMKALGCPDIIFIFGATNDYWAKSPLGEYKYADWSKKDLYSFRPAMAYMLDTMIDYYPNVEIYFLLNDGLGNEIT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 490429420  182 ESVRAICNHYNIDCIELHDIDKKSGHPSIKGMEQISEQIKMFM 224
Cdd:pfam16255 161 ESVRTICKHYQIDCIELKELDKMSGHPSVKGMKQISEQVKAYM 203
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
26-220 9.90e-11

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: 58.96  E-value: 9.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  26 ISILGDSYStfEGYLQPDTNSIWYYVSPRQQTdvtsvkqtwwhkfiKENNYRLCVNNSFSGATIcntgynqADYSDRSFI 105
Cdd:cd00229    1 ILVIGDSIT--AGYGASSGSTFYSLLLYLLLL--------------AGGPGVEVINLGVSGATT-------ADALRRLGL 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420 106 TRMDKLGCPDIIFIFGATNDCWAGSplgdykyegwtKEDLYTFRPAMAYLLDHMIDRYPNVEIYFL----------LNSG 175
Cdd:cd00229   58 RLALLKDKPDLVIIELGTNDLGRGG-----------DTSIDEFKANLEELLDALRERAPGAKVILItppppppregLLGR 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490429420 176 LKEEFNESVRAICNHYNIDC-IELHDIDKKSG------------HPSIKGMEQISEQI 220
Cdd:cd00229  127 ALPRYNEAIKAVAAENPAPSgVDLVDLAALLGdedkslyspdgiHPNPAGHKLIAEAL 184
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
24-220 2.11e-10

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: 58.12  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  24 KSISILGDSYStfEGYLQPDTNSIWYYVSprqqtdvtsvkqtwwhKFIKENNYRLcVNNSFSGATIcntgynqadysdRS 103
Cdd:COG2755    9 LRIVALGDSIT--AGYGASRERGWPALLA----------------RRLAAADVRV-VNAGISGATT------------AD 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420 104 FITRMDKL---GCPDIIFIFGATNDCWAGsplgdykyegwTKEDLYTFRPAMAYLLDHMIDRYPNVEIYFL--------- 171
Cdd:COG2755   58 LLARLDRDllaLKPDLVVIELGTNDLLRG-----------LGVSPEEFRANLEALIDRLRAAGPGARVVLVtppprlrpn 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490429420 172 -LNSGLkEEFNESVRAICNHYNIDCIELHDIDKKSG-----------HPSIKGMEQISEQI 220
Cdd:COG2755  127 yLNERI-EAYNAAIRELAAEYGVPLVDLYAALRDAGdlpdlltadglHPNAAGYRLIAEAV 186
 
Name Accession Description Interval E-value
Lipase_GDSL_lke pfam16255
GDSL-like Lipase/Acylhydrolase;
24-224 8.34e-123

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 435238  Cd Length: 203  Bit Score: 346.70  E-value: 8.34e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420   24 KSISILGDSYSTFEGYLQPDTNSIWYYVSPRQ--QTDVTSVKQTWWHKFIKENNYRLCVNNSFSGATICNTGYNQADYSD 101
Cdd:pfam16255   1 KSVSILGDSYSTFEGYVQPDTNFVWYLKTPPKgrKTDMVSVRNTWWHQFIKENNYRLCVNNSFSGATICHTGYRSEDYSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  102 RSFITRMDKLGCPDIIFIFGATNDCWAGSPLGDYKYEGWTKEDLYTFRPAMAYLLDHMIDRYPNVEIYFLLNSGLKEEFN 181
Cdd:pfam16255  81 RSFITRMKALGCPDIIFIFGATNDYWAKSPLGEYKYADWSKKDLYSFRPAMAYMLDTMIDYYPNVEIYFLLNDGLGNEIT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 490429420  182 ESVRAICNHYNIDCIELHDIDKKSGHPSIKGMEQISEQIKMFM 224
Cdd:pfam16255 161 ESVRTICKHYQIDCIELKELDKMSGHPSVKGMKQISEQVKAYM 203
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
26-220 9.90e-11

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: 58.96  E-value: 9.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  26 ISILGDSYStfEGYLQPDTNSIWYYVSPRQQTdvtsvkqtwwhkfiKENNYRLCVNNSFSGATIcntgynqADYSDRSFI 105
Cdd:cd00229    1 ILVIGDSIT--AGYGASSGSTFYSLLLYLLLL--------------AGGPGVEVINLGVSGATT-------ADALRRLGL 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420 106 TRMDKLGCPDIIFIFGATNDCWAGSplgdykyegwtKEDLYTFRPAMAYLLDHMIDRYPNVEIYFL----------LNSG 175
Cdd:cd00229   58 RLALLKDKPDLVIIELGTNDLGRGG-----------DTSIDEFKANLEELLDALRERAPGAKVILItppppppregLLGR 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490429420 176 LKEEFNESVRAICNHYNIDC-IELHDIDKKSG------------HPSIKGMEQISEQI 220
Cdd:cd00229  127 ALPRYNEAIKAVAAENPAPSgVDLVDLAALLGdedkslyspdgiHPNPAGHKLIAEAL 184
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
24-220 2.11e-10

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: 58.12  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  24 KSISILGDSYStfEGYLQPDTNSIWYYVSprqqtdvtsvkqtwwhKFIKENNYRLcVNNSFSGATIcntgynqadysdRS 103
Cdd:COG2755    9 LRIVALGDSIT--AGYGASRERGWPALLA----------------RRLAAADVRV-VNAGISGATT------------AD 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420 104 FITRMDKL---GCPDIIFIFGATNDCWAGsplgdykyegwTKEDLYTFRPAMAYLLDHMIDRYPNVEIYFL--------- 171
Cdd:COG2755   58 LLARLDRDllaLKPDLVVIELGTNDLLRG-----------LGVSPEEFRANLEALIDRLRAAGPGARVVLVtppprlrpn 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490429420 172 -LNSGLkEEFNESVRAICNHYNIDCIELHDIDKKSG-----------HPSIKGMEQISEQI 220
Cdd:COG2755  127 yLNERI-EAYNAAIRELAAEYGVPLVDLYAALRDAGdlpdlltadglHPNAAGYRLIAEAV 186
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
28-214 3.51e-09

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: 54.47  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420   28 ILGDSYStfEGYLQPDTNSIWyyvsprqqtdvtsvkQTWWHKFIKENNYRLCVNN-SFSGATIcntgynQADYSDRsfIT 106
Cdd:pfam13472   1 ALGDSIT--AGYGATGGDRSY---------------PGWLARLLARRLGADVVNNlGISGATT------RLDLLER--LD 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  107 RMDKLGcPDIIFIFGATNDCWAGSPLGDykyegwtkedlytFRPAMAYLLDHMIDRYPNVEIYFLL-------------- 172
Cdd:pfam13472  56 DVLRLK-PDLVVILLGTNDLGRGVSAAR-------------AAANLEALIDALRAAGPDARVLLIGplpvgpppplderr 121
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 490429420  173 NSGLKEEFNESVRAICNHYNIDCIELHDIDKKSG------------HPSIKGME 214
Cdd:pfam13472 122 LNARIAEYNAAIREVAAERGVPYVDLWDALRDDGgwlpdlladdglHPNAAGYR 175
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
71-220 1.05e-04

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 41.79  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420   71 IKENNYRLCVNNSFSGATICNTGYNQADYSDrsFITRMDKLGCPDIIFIFGATND-CWAGSPLGDYK---------YEGW 140
Cdd:pfam00657  36 VPGSGYNHGANFAIGGATIEDLPIQLEQLLR--LISDVKDQAKPDLVTIFIGANDlCNFLSSPARSKkrvpdlldeLRAN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420  141 TKEDLYTFRPAMAYLLdHMIDRYPNVEIYFLLNSgLKEEFNESVRAICNHY-------NIDCIELHDIDKKSG------- 206
Cdd:pfam00657 114 LPQLGLGARKFWVHGL-GPLGCTPPKGCYELYNA-LAEEYNERLNELVNSLaaaaedaNVVYVDIYGFEDPTDpccgigl 191
                         170
                  ....*....|....*....
gi 490429420  207 -----HPSIKGMEQISEQI 220
Cdd:pfam00657 192 epdglHPSEKGYKAVAEAI 210
Endoglucanase_E_like cd01831
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
113-225 6.30e-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: 39.25  E-value: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490429420 113 CPDIIFIFGATNDCWAGS-PLGDYkyegwtkedlytFRPAMAYLLDHMIDRYPNVEIYFLLNSGLKEEFN-----ESVRA 186
Cdd:cd01831   55 GPDLVVINLGTNDFSTGNnPPGED------------FTNAYVEFIEELRKRYPDAPIVLMLGPMLFGPYGteeeiKRVAE 122
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490429420 187 ICNHYNIDCIELHD---IDKKSG-----HPSIKGMEQISEQIKMFMR 225
Cdd:cd01831  123 AFKDQKSKKVHYFDtpgILQHNDigcdwHPTVAGHQKIAKHLLPAIK 169
 
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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