NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1003701488|ref|NP_001307792|]
View 

isoamyl acetate-hydrolyzing esterase 1 homolog isoform c [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase super family cl01053
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 1-103 2.61e-40

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.


The actual alignment was detected with superfamily member cd01838:

Pssm-ID: 470049  Cd Length: 199  Bit Score: 133.15  E-value: 2.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQD-FSS 79
Cdd:cd01838    97 IVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAMQEEAGwLES 175

                          90       100
                  ....*....|....*....|....
gi 1003701488  80 YLSDGLHLSPKGNEFLFSHLWPLI 103
Cdd:cd01838   176 LLTDGLHFSSKGYELLFEEIVKVI 199
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 1-103 2.61e-40

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: 133.15  E-value: 2.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQD-FSS 79
Cdd:cd01838    97 IVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAMQEEAGwLES 175

                          90       100
                  ....*....|....*....|....
gi 1003701488  80 YLSDGLHLSPKGNEFLFSHLWPLI 103
Cdd:cd01838   176 LLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 1-104 2.98e-11

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: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVDiPENRVILITPTPLCETaweeqciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQDFSSY 80
Cdd:COG2755   101 LIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAEYGVPLVDLYAALRDAGDLPDL 166

                          90       100
                  ....*....|....*....|....*
gi 1003701488  81 LS-DGLHLSPKGNEFLFSHLWPLIE 104
Cdd:COG2755   167 LTaDGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 1-93 5.14e-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: 51.78  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVDiPENRVILITPTPLCETAWEEQciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQD--FS 78
Cdd:pfam13472  90 LIDALRAAG-PDARVLLIGPLPVGPPPPLDE--------RRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGwlPD 160

                          90
                  ....*....|....*
gi 1003701488  79 SYLSDGLHLSPKGNE 93
Cdd:pfam13472 161 LLADDGLHPNAAGYR 175
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 1-103 2.61e-40

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: 133.15  E-value: 2.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQD-FSS 79
Cdd:cd01838    97 IVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAMQEEAGwLES 175

                          90       100
                  ....*....|....*....|....
gi 1003701488  80 YLSDGLHLSPKGNEFLFSHLWPLI 103
Cdd:cd01838   176 LLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 1-104 2.98e-11

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: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVDiPENRVILITPTPLCETaweeqciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQDFSSY 80
Cdd:COG2755   101 LIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAEYGVPLVDLYAALRDAGDLPDL 166

                          90       100
                  ....*....|....*....|....*
gi 1003701488  81 LS-DGLHLSPKGNEFLFSHLWPLIE 104
Cdd:COG2755   167 LTaDGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 1-93 5.14e-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: 51.78  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVDiPENRVILITPTPLCETAWEEQciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQD--FS 78
Cdd:pfam13472  90 LIDALRAAG-PDARVLLIGPLPVGPPPPLDE--------RRLNARIAEYNAAIREVAAERGVPYVDLWDALRDDGGwlPD 160

                          90
                  ....*....|....*
gi 1003701488  79 SYLSDGLHLSPKGNE 93
Cdd:pfam13472 161 LLADDGLHPNAAGYR 175
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
14-99 1.44e-08

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 51.03  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488  14 RVILITPTPLCETAWEEqciIQGCKLNRLNSVVGEYANAclqvAQDCGTDVLDLWTLMQDSQDFSSY--LSDGLHLSPKG 91
Cdd:pfam00657 130 GPLGCTPPKGCYELYNA---LAEEYNERLNELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIglEPDGLHPSEKG 202


                  ....*...
gi 1003701488  92 NEFLFSHL 99
Cdd:pfam00657 203 YKAVAEAI 210
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 1-107 2.65e-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.


Pssm-ID: 239945  Cd Length: 183  Bit Score: 47.32  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVDIpenRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYanaclqvAQDCGTDVLDLWTLMQDSQDF--- 77
Cdd:cd04501    88 MVELAEANGI---KVILASPLPVDDYPWKPQWLRPANKLKSLNRWLKDY-------ARENGLLFLDFYSPLLDERNVglk 157

                          90       100       110
                  ....*....|....*....|....*....|
gi 1003701488  78 SSYLSDGLHLSPKGNEFLFshlwPLIEKKV 107
Cdd:cd04501   158 PGLLTDGLHPSREGYRVMA----PLAEKAL 183
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 1-102 1.17e-04

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: 40.09  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701488   1 MVQYLKSVDiPENRVILITPTPLceTAWEEQCIIQGCKLNRLNSVVGEYANACLQVaqdcgtDVLDLWTLMQDsQDFSSY 80
Cdd:cd00229    96 LLDALRERA-PGAKVILITPPPP--PPREGLLGRALPRYNEAIKAVAAENPAPSGV------DLVDLAALLGD-EDKSLY 165

                          90       100
                  ....*....|....*....|..
gi 1003701488  81 LSDGLHLSPKGNEFLFSHLWPL 102
Cdd:cd00229   166 SPDGIHPNPAGHKLIAEALASA 187
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 38-102 3.39e-03

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: 35.71  E-value: 3.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003701488  38 KLNRLNSVVGEyanaclqVAQDCGTDVLDLWTL--MQDSQDFSSylsDGLHLSPKGNEFLFSHLWPL 102
Cdd:cd01832   129 RLAAYNAVIRA-------VAARYGAVHVDLWEHpeFADPRLWAS---DRLHPSAAGHARLAALVLAA 185
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH