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Conserved domains on  [gi|1896028742|ref|WP_186433177|]
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SGNH/GDSL hydrolase family protein [Oenococcus oeni]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110757)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Endoglucanase_E_like cd01831
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
136-316 1.92e-29

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: 110.51  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 136 FIGDSIINGQKILPDS---FDTSAHRPDKSWAYLLSEKLDFNNLRIAYGGTGitqraniypptaidfiwnsalnvsrpid 212
Cdd:cd01831     4 FIGDSITCGYGVTGKSrcdFSAATEDPSLSYAALLARALNAEYSIIAYSGIG---------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 213 ysqpLAGVIVNLGTNDRSA----RSEEFSFSLKALLRELKKRFHETKIIVVE-PF------NGCFQDVFRKVFKDEKHiS 281
Cdd:cd01831    56 ----PDLVVINLGTNDFSTgnnpPGEDFTNAYVEFIEELRKRYPDAPIVLMLgPMlfgpygTEEEIKRVAEAFKDQKS-K 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1896028742 282 LIENNHW----NFEISDHGVHLSVTGQQQAAKTLLPLIE 316
Cdd:cd01831   131 KVHYFDTpgilQHNDIGCDWHPTVAGHQKIAKHLLPAIK 169
 
Name Accession Description Interval E-value
Endoglucanase_E_like cd01831
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
136-316 1.92e-29

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: 110.51  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 136 FIGDSIINGQKILPDS---FDTSAHRPDKSWAYLLSEKLDFNNLRIAYGGTGitqraniypptaidfiwnsalnvsrpid 212
Cdd:cd01831     4 FIGDSITCGYGVTGKSrcdFSAATEDPSLSYAALLARALNAEYSIIAYSGIG---------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 213 ysqpLAGVIVNLGTNDRSA----RSEEFSFSLKALLRELKKRFHETKIIVVE-PF------NGCFQDVFRKVFKDEKHiS 281
Cdd:cd01831    56 ----PDLVVINLGTNDFSTgnnpPGEDFTNAYVEFIEELRKRYPDAPIVLMLgPMlfgpygTEEEIKRVAEAFKDQKS-K 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1896028742 282 LIENNHW----NFEISDHGVHLSVTGQQQAAKTLLPLIE 316
Cdd:cd01831   131 KVHYFDTpgilQHNDIGCDWHPTVAGHQKIAKHLLPAIK 169
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
125-316 9.06e-12

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: 63.12  E-value: 9.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 125 TGAVPSRKNLVFIGDSIINGQKIlpdsfdtsahRPDKSWAYLLSEKLDFNNLRI---AYGGTgitqraniyppTAIDFI- 200
Cdd:COG2755     2 KAAAGKPLRIVALGDSITAGYGA----------SRERGWPALLARRLAAADVRVvnaGISGA-----------TTADLLa 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 201 -WNSALNVSRPiDYsqplagVIVNLGTND----RSARSEEFSFSLKALLRELKKRFHETKIIVVE--PFNGC-------- 265
Cdd:COG2755    61 rLDRDLLALKP-DL------VVIELGTNDllrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTppPRLRPnylnerie 133
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1896028742 266 -FQDVFRKVFKDEK-------HISLIENNHWNFEISDhGVHLSVTGQQQAAKTLLPLIE 316
Cdd:COG2755   134 aYNAAIRELAAEYGvplvdlyAALRDAGDLPDLLTAD-GLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
136-305 2.70e-10

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: 58.33  E-value: 2.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 136 FIGDSIINGqkilpdSFDTSAHRPDKSW-AYLLSEKLDF---NNLriAYGGTGITQRANIYPPTAIDFiwnsalnvsRPi 211
Cdd:pfam13472   1 ALGDSITAG------YGATGGDRSYPGWlARLLARRLGAdvvNNL--GISGATTRLDLLERLDDVLRL---------KP- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 212 DYsqplagVIVNLGTND--RSARSEEFSFSLKALLRELKKRFHETKIIVVEPFNGC----------------FQDVFRKV 273
Cdd:pfam13472  63 DL------VVILLGTNDlgRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGpppplderrlnariaeYNAAIREV 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1896028742 274 fKDEKHISLI--------ENNHWNFEISDHGVHLSVTGQQ 305
Cdd:pfam13472 137 -AAERGVPYVdlwdalrdDGGWLPDLLADDGLHPNAAGYR 175
 
Name Accession Description Interval E-value
Endoglucanase_E_like cd01831
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
136-316 1.92e-29

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: 110.51  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 136 FIGDSIINGQKILPDS---FDTSAHRPDKSWAYLLSEKLDFNNLRIAYGGTGitqraniypptaidfiwnsalnvsrpid 212
Cdd:cd01831     4 FIGDSITCGYGVTGKSrcdFSAATEDPSLSYAALLARALNAEYSIIAYSGIG---------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 213 ysqpLAGVIVNLGTNDRSA----RSEEFSFSLKALLRELKKRFHETKIIVVE-PF------NGCFQDVFRKVFKDEKHiS 281
Cdd:cd01831    56 ----PDLVVINLGTNDFSTgnnpPGEDFTNAYVEFIEELRKRYPDAPIVLMLgPMlfgpygTEEEIKRVAEAFKDQKS-K 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1896028742 282 LIENNHW----NFEISDHGVHLSVTGQQQAAKTLLPLIE 316
Cdd:cd01831   131 KVHYFDTpgilQHNDIGCDWHPTVAGHQKIAKHLLPAIK 169
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
125-316 9.06e-12

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: 63.12  E-value: 9.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 125 TGAVPSRKNLVFIGDSIINGQKIlpdsfdtsahRPDKSWAYLLSEKLDFNNLRI---AYGGTgitqraniyppTAIDFI- 200
Cdd:COG2755     2 KAAAGKPLRIVALGDSITAGYGA----------SRERGWPALLARRLAAADVRVvnaGISGA-----------TTADLLa 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 201 -WNSALNVSRPiDYsqplagVIVNLGTND----RSARSEEFSFSLKALLRELKKRFHETKIIVVE--PFNGC-------- 265
Cdd:COG2755    61 rLDRDLLALKP-DL------VVIELGTNDllrgLGVSPEEFRANLEALIDRLRAAGPGARVVLVTppPRLRPnylnerie 133
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1896028742 266 -FQDVFRKVFKDEK-------HISLIENNHWNFEISDhGVHLSVTGQQQAAKTLLPLIE 316
Cdd:COG2755   134 aYNAAIRELAAEYGvplvdlyAALRDAGDLPDLLTAD-GLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
136-305 2.70e-10

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: 58.33  E-value: 2.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 136 FIGDSIINGqkilpdSFDTSAHRPDKSW-AYLLSEKLDF---NNLriAYGGTGITQRANIYPPTAIDFiwnsalnvsRPi 211
Cdd:pfam13472   1 ALGDSITAG------YGATGGDRSYPGWlARLLARRLGAdvvNNL--GISGATTRLDLLERLDDVLRL---------KP- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 212 DYsqplagVIVNLGTND--RSARSEEFSFSLKALLRELKKRFHETKIIVVEPFNGC----------------FQDVFRKV 273
Cdd:pfam13472  63 DL------VVILLGTNDlgRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGpppplderrlnariaeYNAAIREV 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1896028742 274 fKDEKHISLI--------ENNHWNFEISDHGVHLSVTGQQ 305
Cdd:pfam13472 137 -AAERGVPYVdlwdalrdDGGWLPDLLADDGLHPNAAGYR 175
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
132-312 2.35e-05

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: 44.21  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 132 KNLVFIGDSIINGQKiLPDSFDTSAH--RPDKswayllseKLDFNNLriAYGGTGITQRANIYPPTAIDFiwnsalnvsr 209
Cdd:cd01834     2 DRIVFIGNSITDRGG-YVGYVETYLAarYPEL--------KLTFRNL--GWSGDTVSDLAARRDRDVLPA---------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 210 pidysQPLAgVIVNLGTND------RSARSEEFSFSLKALLRELKKRFHETKIIVVEPF-------NGCFQDVFRKVFK- 275
Cdd:cd01834    61 -----KPDV-VSIMFGINDsfrgfdDPVGLEKFKTNLRRLIDRLKNKESAPRIVLVSPIayeanedPLPDGAEYNANLAa 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1896028742 276 ---------DEKHISLIENNHWNFEI---------SDHGVHLSVTGQQQAAKTLL 312
Cdd:cd01834   135 yadavrelaAENGVAFVDLFTPMKEAfqkageavlTVDGVHPNEAGHRALARLWL 189
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
134-314 4.93e-05

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: 43.56  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 134 LVFIGDSIINGqkilPDSFDTSAHRPDKSWAYLLSEKLDFNNLRIAYGGTGITQraniypptAIDFIWNSALNVSRPIDY 213
Cdd:cd00229     1 ILVIGDSITAG----YGASSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTAD--------ALRRLGLRLALLKDKPDL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896028742 214 sqplagVIVNLGTNDRSARS----EEFSFSLKALLRELKKRFHETKIIVVEPF------------NGCFQDVFRKVFKDE 277
Cdd:cd00229    69 ------VIIELGTNDLGRGGdtsiDEFKANLEELLDALRERAPGAKVILITPPppppregllgraLPRYNEAIKAVAAEN 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1896028742 278 KHISLIENNHWNFEISDH--------GVHLSVTGQQQAAKTLLPL 314
Cdd:cd00229   143 PAPSGVDLVDLAALLGDEdkslyspdGIHPNPAGHKLIAEALASA 187
 
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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