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Conserved domains on  [gi|568977936|ref|XP_006515239|]
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isoamyl acetate-hydrolyzing esterase 1 homolog isoform X2 [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 ...
 17-153 1.57e-63

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: 195.55  E-value: 1.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  17 RVLLFGDSITQFSFQQG--GWGSLLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGPgMENPVAVTIFFGANDSSLK 94
Cdd:cd01838    1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEK-LAQPDLVTIFFGANDAALP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568977936  95 DENpkQHVPLDEYSANLRDMVQYLRSVdVPRERVILITPPPLCEAAWEKECVLKAGQPG 153
Cdd:cd01838   80 GQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPG 135
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 17-153 1.57e-63

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: 195.55  E-value: 1.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  17 RVLLFGDSITQFSFQQG--GWGSLLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGPgMENPVAVTIFFGANDSSLK 94
Cdd:cd01838    1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEK-LAQPDLVTIFFGANDAALP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568977936  95 DENpkQHVPLDEYSANLRDMVQYLRSVdVPRERVILITPPPLCEAAWEKECVLKAGQPG 153
Cdd:cd01838   80 GQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPG 135
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
18-144 3.27e-23

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 92.25  E-value: 3.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936   18 VLLFGDSITQFSFQQGG----WGSLLADRLVRKCDVLNrgfSGYNTRWAKII--------------LPRLIRKGPGMENP 79
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPG---SGYNHGANFAIggatiedlpiqleqLLRLISDVKDQAKP 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936   80 VAVTIFFGAND-----SSLKDENPKQHVPLDEYSANLRDMVQYLRSVDVPRERVILITPPPLCEAAWEKE 144
Cdd:pfam00657  78 DLVTIFIGANDlcnflSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNAL 147
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 16-135 9.56e-20

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: 82.77  E-value: 9.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  16 PRVLLFGDSITQ--FSFQQGGWGSLLADRL-VRKCDVLNRGFSGYNTRWakiILPRLIRKGPGMeNPVAVTIFFGANDSs 92
Cdd:COG2755    9 LRIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLAL-KPDLVVIELGTNDL- 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568977936  93 lkdeNPKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPP 135
Cdd:COG2755   84 ----LRGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPP 121
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 17-153 1.57e-63

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: 195.55  E-value: 1.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  17 RVLLFGDSITQFSFQQG--GWGSLLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGPgMENPVAVTIFFGANDSSLK 94
Cdd:cd01838    1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEK-LAQPDLVTIFFGANDAALP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568977936  95 DENpkQHVPLDEYSANLRDMVQYLRSVdVPRERVILITPPPLCEAAWEKECVLKAGQPG 153
Cdd:cd01838   80 GQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPG 135
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
18-144 3.27e-23

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 92.25  E-value: 3.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936   18 VLLFGDSITQFSFQQGG----WGSLLADRLVRKCDVLNrgfSGYNTRWAKII--------------LPRLIRKGPGMENP 79
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPG---SGYNHGANFAIggatiedlpiqleqLLRLISDVKDQAKP 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936   80 VAVTIFFGAND-----SSLKDENPKQHVPLDEYSANLRDMVQYLRSVDVPRERVILITPPPLCEAAWEKE 144
Cdd:pfam00657  78 DLVTIFIGANDlcnflSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNAL 147
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 16-135 9.56e-20

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: 82.77  E-value: 9.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  16 PRVLLFGDSITQ--FSFQQGGWGSLLADRL-VRKCDVLNRGFSGYNTRWakiILPRLIRKGPGMeNPVAVTIFFGANDSs 92
Cdd:COG2755    9 LRIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLAL-KPDLVVIELGTNDL- 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568977936  93 lkdeNPKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPP 135
Cdd:COG2755   84 ----LRGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPP 121
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 20-149 3.42e-16

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: 72.96  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936   20 LFGDSITQ---FSFQQGGWGSLLADRLVRKCD---VLNRGFSGYNTRwaKIILPRLIRKGPgmENPVAVTIFFGANDSsl 93
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLARRLGadvVNNLGISGATTR--LDLLERLDDVLR--LKPDLVVILLGTNDL-- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568977936   94 kdenpKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPPLCEAAWEKECVLKA 149
Cdd:pfam13472  75 -----GRGVSAARAAANLEALIDALRAAG-PDARVLLIGPLPVGPPPPLDERRLNA 124
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 17-136 1.17e-12

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: 63.85  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  17 RVLLFGDSITQfsfqQGGWGSLLADRLV-----RKCDVLNRGFSGYNT-----RWAKIILPRlirkgpgmeNPVAVTIFF 86
Cdd:cd01834    3 RIVFIGNSITD----RGGYVGYVETYLAarypeLKLTFRNLGWSGDTVsdlaaRRDRDVLPA---------KPDVVSIMF 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568977936  87 GANDSslkDENPKQHVPLDEYSANLRDMVQYLRSvDVPRERVILITPPPL 136
Cdd:cd01834   70 GINDS---FRGFDDPVGLEKFKTNLRRLIDRLKN-KESAPRIVLVSPIAY 115
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 18-135 1.25e-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: 60.89  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  18 VLLFGDSITQ---FSFQQGGWGSLLADRLVRKCD---VLNRGFSGYNTRWAKIILPRLIRKGPgmENPVAVTIFFGANDS 91
Cdd:cd00229    1 ILVIGDSITAgygASSGSTFYSLLLYLLLLAGGPgveVINLGVSGATTADALRRLGLRLALLK--DKPDLVIIELGTNDL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568977936  92 slkdeNPKQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPP 135
Cdd:cd00229   79 -----GRGGDTSIDEFKANLEELLDALRERA-PGAKVILITPPP 116
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 16-135 1.96e-11

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: 60.69  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  16 PRVLLFGDSITQ---FSFQQGGWGSLLADRLVRKCDVLNRGFSGYNTR-------WAKIIlpRLIRKGPgmenpvAVTIF 85
Cdd:cd01821    1 PTIFLAGDSTVAdydPGAPQAGWGQALPQYLDTGITVVNHAKGGRSSRsfrdegrWDAIL--KLIKPGD------YVLIQ 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977936  86 FGANDSslKDENPKQHVPLDEYSANLRDMVQylrsvDVpRER---VILITPPP 135
Cdd:cd01821   73 FGHNDQ--KPKDPEYTEPYTTYKEYLRRYIA-----EA-RAKgatPILVTPVT 117
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 17-135 1.10e-08

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: 52.28  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  17 RVLLFGDSITQFsfqqGGWGSLLADRlvrkcDVLNRGFSGYNTRWakiILPRL--IRKGpgmeNPVAVTIFFGANDSSlk 94
Cdd:cd01828    1 ALVFLGDSLTEG----GPWALLFPDV-----KVANRGISGDTTRG---LLARLdeDVAL----QPKAIFIMIGINDLA-- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568977936  95 denpkQHVPLDEYSANLRDMVQYLRSVDvPRERVILITPPP 135
Cdd:cd01828   63 -----QGTSDEDIVANYRTILEKLRKHF-PNIKIVVQSILP 97
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 16-131 2.04e-08

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: 51.74  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  16 PRVLLFGDSITQ-FSFQQG-GWGSLLADRLVRKC---DVLNRGFSGYNTRWAKIILPRLIRKgpgmENPVAVTIFFGAND 90
Cdd:cd01822    1 VTILALGDSLTAgYGLPPEeGWPALLQKRLDARGidvTVINAGVSGDTTAGGLARLPALLAQ----HKPDLVILELGGND 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568977936  91 SslkdenpKQHVPLDEYSANLRDMVQYLRSVDVPrerVILI 131
Cdd:cd01822   77 G-------LRGIPPDQTRANLRQMIETAQARGAP---VLLV 107
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 17-143 1.19e-05

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: 44.24  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  17 RVLLFGDSITQfsfqqgGWGSLLADRLVRKCD------VLNRGFSGYNTRWakiILPR----LIRkgpgmENPVAVTIFF 86
Cdd:cd04501    2 RVVCLGDSITY------GYPVGPEASWVNLLAeflgkeVINRGINGDTTSQ---MLVRfyedVIA-----LKPAVVIIMG 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568977936  87 GANDSSlkdenpkQHVPLDEYSANLRDMVQYLRSVDVpreRVILITPPPLCEAAWEK 143
Cdd:cd04501   68 GTNDII-------VNTSLEMIKDNIRSMVELAEANGI---KVILASPLPVDDYPWKP 114
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 19-144 6.80e-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: 41.93  E-value: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977936  19 LLFGDSITQFSFQQGGWGSLladrlvrkCDVLNRGFSGYNTRWA-KIILPRLIRKgpgmeNPVAVTIFFGANDSSLKden 97
Cdd:cd01841    4 VFIGDSLFEGWPLYEAEGKG--------KTVNNLGIAGISSRQYlEHIEPQLIQK-----NPSKVFLFLGTNDIGKE--- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568977936  98 pkqhVPLDEYSANLRDMVQYLRSvDVPRERVILITPPPLCEAAWEKE 144
Cdd:cd01841   68 ----VSSNQFIKWYRDIIEQIRE-EFPNTKIYLLSVLPVLEEDEIKT 109
 
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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