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Conserved domains on  [gi|568977938|ref|XP_006515240|]
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isoamyl acetate-hydrolyzing esterase 1 homolog isoform X3 [Mus musculus]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110876)

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
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 3-135 2.12e-60

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases 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 Ser-His-Asp(Glu) triad found in other serine hydrolases


:

Pssm-ID: 238876  Cd Length: 199  Bit Score: 185.92  E-value: 2.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSSLKDENpkQHVPLDEYSANLRDMVQYLRSVdVPRERVILITPPPLCEAAWEKECVLKGCKLNRLNS 82
Cdd:cd01838   63 QPDLVTIFFGANDAALPGQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNE 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977938  83 VVGEYANACLQVARDCGTDVLDLWTLMQKDSQDFSSYLSDGLHLSPMGNEFLF 135
Cdd:cd01838  140 LLKQYAEACVEVAEELGVPVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLF 192
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 3-135 2.12e-60

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases 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 Ser-His-Asp(Glu) triad found in other serine hydrolases


Pssm-ID: 238876  Cd Length: 199  Bit Score: 185.92  E-value: 2.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSSLKDENpkQHVPLDEYSANLRDMVQYLRSVdVPRERVILITPPPLCEAAWEKECVLKGCKLNRLNS 82
Cdd:cd01838   63 QPDLVTIFFGANDAALPGQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNE 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977938  83 VVGEYANACLQVARDCGTDVLDLWTLMQKDSQDFSSYLSDGLHLSPMGNEFLF 135
Cdd:cd01838  140 LLKQYAEACVEVAEELGVPVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLF 192
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
2-135 1.04e-19

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 81.85  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938    2 ENPVAVTIFFGAND-----SSLKDENPKQHVPLDEYSANLRDMVQYLRSVDVPRERVILITPPPLCEAAWEKEcvlKGCK 76
Cdd:pfam00657  75 AKPDLVTIFIGANDlcnflSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNAL---AEEY 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   77 LNRLNSVVGEYANAclqvARDCGTDVLDLWTLMQKDSQDFSSYLS-DGLHLSPMGNEFLF 135
Cdd:pfam00657 152 NERLNELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVA 207
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 3-142 3.68e-18

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: 77.38  E-value: 3.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSslkdeNPKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPPLCEAawekecvlkgcklNRLNS 82
Cdd:COG2755   70 KPDLVVIELGTNDL-----LRGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNE 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938  83 VVGEYANACLQVARDCGTDVLDLWTLMQKDSQDFSSYLSDGLHLSPMGNEFLFLNLCPLL 142
Cdd:COG2755  131 RIEAYNAAIRELAAEYGVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 3-135 2.12e-60

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases 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 Ser-His-Asp(Glu) triad found in other serine hydrolases


Pssm-ID: 238876  Cd Length: 199  Bit Score: 185.92  E-value: 2.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSSLKDENpkQHVPLDEYSANLRDMVQYLRSVdVPRERVILITPPPLCEAAWEKECVLKGCKLNRLNS 82
Cdd:cd01838   63 QPDLVTIFFGANDAALPGQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNE 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977938  83 VVGEYANACLQVARDCGTDVLDLWTLMQKDSQDFSSYLSDGLHLSPMGNEFLF 135
Cdd:cd01838  140 LLKQYAEACVEVAEELGVPVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLF 192
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
2-135 1.04e-19

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 81.85  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938    2 ENPVAVTIFFGAND-----SSLKDENPKQHVPLDEYSANLRDMVQYLRSVDVPRERVILITPPPLCEAAWEKEcvlKGCK 76
Cdd:pfam00657  75 AKPDLVTIFIGANDlcnflSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNAL---AEEY 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   77 LNRLNSVVGEYANAclqvARDCGTDVLDLWTLMQKDSQDFSSYLS-DGLHLSPMGNEFLF 135
Cdd:pfam00657 152 NERLNELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVA 207
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 3-142 3.68e-18

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: 77.38  E-value: 3.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSslkdeNPKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPPLCEAawekecvlkgcklNRLNS 82
Cdd:COG2755   70 KPDLVVIELGTNDL-----LRGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNE 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938  83 VVGEYANACLQVARDCGTDVLDLWTLMQKDSQDFSSYLSDGLHLSPMGNEFLFLNLCPLL 142
Cdd:COG2755  131 RIEAYNAAIRELAAEYGVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 3-132 7.55e-18

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: 76.43  E-value: 7.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938    3 NPVAVTIFFGANDSslkdenpKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPPLCEAAWEKEcvlkgcklNRLNS 82
Cdd:pfam13472  61 KPDLVVILLGTNDL-------GRGVSAARAAANLEALIDALRAAG-PDARVLLIGPLPVGPPPPLDE--------RRLNA 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568977938   83 VVGEYANACLQVARDCGTDVLDLWTLMQKDSQDFSSYLS-DGLHLSPMGNE 132
Cdd:pfam13472 125 RIAEYNAAIREVAAERGVPYVDLWDALRDDGGWLPDLLAdDGLHPNAAGYR 175
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 2-134 5.01e-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: 58.58  E-value: 5.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   2 ENPVAVTIFFGANDSslkdeNPKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPPLCEAAWekecvLKGCKLNRLN 81
Cdd:cd00229   64 DKPDLVIIELGTNDL-----GRGGDTSIDEFKANLEELLDALRERA-PGAKVILITPPPPPPREG-----LLGRALPRYN 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977938  82 SVVGEYANACLQVARDcgtDVLDLWTLMQKDSQDFssYLSDGLHLSPMGNEFL 134
Cdd:cd00229  133 EAIKAVAAENPAPSGV---DLVDLAALLGDEDKSL--YSPDGIHPNPAGHKLI 180
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 3-130 5.32e-11

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: 58.46  E-value: 5.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSslkDENPKQHVPLDEYSANLRDMVQYLRSvDVPRERVILITPPPLcEAAWEKECVLKGcklnrLNS 82
Cdd:cd01834   61 KPDVVSIMFGINDS---FRGFDDPVGLEKFKTNLRRLIDRLKN-KESAPRIVLVSPIAY-EANEDPLPDGAE-----YNA 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568977938  83 VVGEYANACLQVARDCGTDVLDLWTLMQK--DSQDFSSYLSDGLHLSPMG 130
Cdd:cd01834  131 NLAAYADAVRELAAENGVAFVDLFTPMKEafQKAGEAVLTVDGVHPNEAG 180
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 2-135 1.22e-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.


Pssm-ID: 239945  Cd Length: 183  Bit Score: 51.94  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   2 ENPVAVTIFFGANDSSlkdenpkQHVPLDEYSANLRDMVQYLRSVDVpreRVILITPPPLCEAAWEKECVLKGCKLNRLN 81
Cdd:cd04501   58 LKPAVVIIMGGTNDII-------VNTSLEMIKDNIRSMVELAEANGI---KVILASPLPVDDYPWKPQWLRPANKLKSLN 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568977938  82 SVVGEYanaclqvARDCGTDVLDLWT-LMQKDSQDFSS-YLSDGLHLSPMGNEFLF 135
Cdd:cd04501  128 RWLKDY-------ARENGLLFLDFYSpLLDERNVGLKPgLLTDGLHPSREGYRVMA 176
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 7-130 1.80e-07

Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.


Pssm-ID: 238859  Cd Length: 198  Bit Score: 48.75  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   7 VTIFFGANDSslKDENPKQHVPLDEYSANLRDMVQylrsvDVpRER---VILITPPPlcEAAWEKEcvlkgcklNRLNSV 83
Cdd:cd01821   69 VLIQFGHNDQ--KPKDPEYTEPYTTYKEYLRRYIA-----EA-RAKgatPILVTPVT--RRTFDEG--------GKVEDT 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568977938  84 VGEYANACLQVARDCGTDVLDLWTLM---------QKDSQDFSSYLSDGLHLSPMG 130
Cdd:cd01821  131 LGDYPAAMRELAAEEGVPLIDLNAASralyeaigpEKSKKYFPEGPGDNTHFSEKG 186
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 3-130 1.93e-07

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: 48.43  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSSlkdenpkQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPPLceaawekecvlkGCKLNRLNS 82
Cdd:cd01828   48 QPKAIFIMIGINDLA-------QGTSDEDIVANYRTILEKLRKHF-PNIKIVVQSILPV------------GELKSIPNE 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568977938  83 VVGEyANACL-QVARDCGTDVLDLWT-LMQKDSQDFSSYLSDGLHLSPMG 130
Cdd:cd01828  108 QIEE-LNRQLaQLAQQEGVTFLDLWAvFTNADGDLKNEFTTDGLHLNAKG 156
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 7-141 7.98e-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. 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: 7.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   7 VTIFFGANDSSlkdeNPKqhVPLDEYSANLRDMVQYLRsvdVPRERVILITPPPLceAAWEKECVLKGCKLNRLNSVVGE 86
Cdd:cd01832   71 VTLLAGGNDIL----RPG--TDPDTYRADLEEAVRRLR---AAGARVVVFTIPDP--AVLEPFRRRVRARLAAYNAVIRA 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568977938  87 yanaclqVARDCGTDVLDLWTLMQ-KDSQDFSSylsDGLHLSPMGNEFLFLNLCPL 141
Cdd:cd01832  140 -------VAARYGAVHVDLWEHPEfADPRLWAS---DRLHPSAAGHARLAALVLAA 185
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 3-134 2.05e-05

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: 42.70  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977938   3 NPVAVTIFFGANDSSLKdenpkqhVPLDEYSANLRDMVQYLRSvDVPRERVILITPPPLCEAAWEKEcvlkgcklnRLNS 82
Cdd:cd01841   51 NPSKVFLFLGTNDIGKE-------VSSNQFIKWYRDIIEQIRE-EFPNTKIYLLSVLPVLEEDEIKT---------RSNT 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977938  83 VVGEYANACLQVARDCGTDVLDLWT-LMQKDSQDFSSYLSDGLHLSPMGNEFL 134
Cdd:cd01841  114 RIQRLNDAIKELAPELGVTFIDLNDvLVDEFGNLKKEYTTDGLHFNPKGYQKL 166
 
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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