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Conserved domains on  [gi|88853865|ref|NP_001034702|]
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isoamyl acetate-hydrolyzing esterase 1 homolog isoform a [Homo sapiens]

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 ...
 17-216 7.50e-97

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: 281.45  E-value: 7.50e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  17 RLLLFGDSITQFSFQQG--GWGASLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGnSLDIPVAVTIFFGANDSALK 94
Cdd:cd01838   1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEE-KLAQPDLVTIFFGANDAALP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  95 DENpkQHIPLEEYAANLKSMVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCG 174
Cdd:cd01838  80 GQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 88853865 175 TDVLDLWTLMQDSQD-FSSYLSDGLHLSPKGNEFLFSHLWPLI 216
Cdd:cd01838 157 VPVIDLWTAMQEEAGwLESLLTDGLHFSSKGYELLFEEIVKVI 199
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 17-216 7.50e-97

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: 281.45  E-value: 7.50e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  17 RLLLFGDSITQFSFQQG--GWGASLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGnSLDIPVAVTIFFGANDSALK 94
Cdd:cd01838   1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEE-KLAQPDLVTIFFGANDAALP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  95 DENpkQHIPLEEYAANLKSMVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCG 174
Cdd:cd01838  80 GQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 88853865 175 TDVLDLWTLMQDSQD-FSSYLSDGLHLSPKGNEFLFSHLWPLI 216
Cdd:cd01838 157 VPVIDLWTAMQEEAGwLESLLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 16-217 1.63e-32

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: 117.05  E-value: 1.63e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  16 PRLLLFGDSITQ--FSFQQGGWGASLADRL-VRKCDVLNRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFFGANDSA 92
Cdd:COG2755   9 LRIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLALK-PDLVVIELGTNDLL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  93 lkdenPKQHIPLEEYAANLKSMVQYLKSVDiPENRVILITPTPLCETaweeqciiqgcklNRLNSVVGEYANACLQVAQD 172
Cdd:COG2755  85 -----RGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAE 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 88853865 173 CGTDVLDLWTLMQDSQDFSSYLS-DGLHLSPKGNEFLFSHLWPLIE 217
Cdd:COG2755 146 YGVPLVDLYAALRDAGDLPDLLTaDGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
18-212 3.01e-31

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 114.59  E-value: 3.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865    18 LLLFGDSITQFSFQQGG----WGASLADRLVRKCDVLNrgfSGYNTRWAKII--------------LPRLIRKGNSLDIP 79
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPG---SGYNHGANFAIggatiedlpiqleqLLRLISDVKDQAKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865    80 VAVTIFFGAND--SALKDENPK---QHIPLEEYAANLKSMVQYLKSVDIPENRVILITPTPLCETAWEEqciIQGCKLNR 154
Cdd:pfam00657  78 DLVTIFIGANDlcNFLSSPARSkkrVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNA---LAEEYNER 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865   155 LNSVVGEYANAclqvAQDCGTDVLDLWTLMQDSQDFSSY--LSDGLHLSPKGNEFLFSHL 212
Cdd:pfam00657 155 LNELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIglEPDGLHPSEKGYKAVAEAI 210
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 17-216 7.50e-97

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: 281.45  E-value: 7.50e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  17 RLLLFGDSITQFSFQQG--GWGASLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGnSLDIPVAVTIFFGANDSALK 94
Cdd:cd01838   1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEE-KLAQPDLVTIFFGANDAALP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  95 DENpkQHIPLEEYAANLKSMVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCG 174
Cdd:cd01838  80 GQP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 88853865 175 TDVLDLWTLMQDSQD-FSSYLSDGLHLSPKGNEFLFSHLWPLI 216
Cdd:cd01838 157 VPVIDLWTAMQEEAGwLESLLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 16-217 1.63e-32

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: 117.05  E-value: 1.63e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  16 PRLLLFGDSITQ--FSFQQGGWGASLADRL-VRKCDVLNRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFFGANDSA 92
Cdd:COG2755   9 LRIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLALK-PDLVVIELGTNDLL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  93 lkdenPKQHIPLEEYAANLKSMVQYLKSVDiPENRVILITPTPLCETaweeqciiqgcklNRLNSVVGEYANACLQVAQD 172
Cdd:COG2755  85 -----RGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAE 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 88853865 173 CGTDVLDLWTLMQDSQDFSSYLS-DGLHLSPKGNEFLFSHLWPLIE 217
Cdd:COG2755 146 YGVPLVDLYAALRDAGDLPDLLTaDGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
18-212 3.01e-31

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 114.59  E-value: 3.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865    18 LLLFGDSITQFSFQQGG----WGASLADRLVRKCDVLNrgfSGYNTRWAKII--------------LPRLIRKGNSLDIP 79
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPG---SGYNHGANFAIggatiedlpiqleqLLRLISDVKDQAKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865    80 VAVTIFFGAND--SALKDENPK---QHIPLEEYAANLKSMVQYLKSVDIPENRVILITPTPLCETAWEEqciIQGCKLNR 154
Cdd:pfam00657  78 DLVTIFIGANDlcNFLSSPARSkkrVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNA---LAEEYNER 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865   155 LNSVVGEYANAclqvAQDCGTDVLDLWTLMQDSQDFSSY--LSDGLHLSPKGNEFLFSHL 212
Cdd:pfam00657 155 LNELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIglEPDGLHPSEKGYKAVAEAI 210
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 20-206 6.54e-27

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: 102.24  E-value: 6.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865    20 LFGDSITQ---FSFQQGGWGASLADRLVRKCD---VLNRGFSGYNTRwakIILPRLIRKGNSLDiPVAVTIFFGANDSAl 93
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLARRLGadvVNNLGISGATTR---LDLLERLDDVLRLK-PDLVVILLGTNDLG- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865    94 kdenpkQHIPLEEYAANLKSMVQYLKSVDiPENRVILITPTPLCETAWEEQciiqgcklNRLNSVVGEYANACLQVAQDC 173
Cdd:pfam13472  76 ------RGVSAARAAANLEALIDALRAAG-PDARVLLIGPLPVGPPPPLDE--------RRLNARIAEYNAAIREVAAER 140

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 88853865   174 GTDVLDLWTLMQDSQD--FSSYLSDGLHLSPKGNE 206
Cdd:pfam13472 141 GVPYVDLWDALRDDGGwlPDLLADDGLHPNAAGYR 175
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 18-215 5.47e-18

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: 78.99  E-value: 5.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  18 LLLFGDSITQ---FSFQQGGWGASLADRLVRKCD---VLNRGFSGYNTRWAKIIL-PRLIRKGNSLDIpvaVTIFFGAND 90
Cdd:cd00229   1 ILVIGDSITAgygASSGSTFYSLLLYLLLLAGGPgveVINLGVSGATTADALRRLgLRLALLKDKPDL---VIIELGTND 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  91 SALKdenpkQHIPLEEYAANLKSMVQYLKSVDiPENRVILITPTPLceTAWEEQCIIQGCKLNRLNSVVGEYANACLQVa 170
Cdd:cd00229  78 LGRG-----GDTSIDEFKANLEELLDALRERA-PGAKVILITPPPP--PPREGLLGRALPRYNEAIKAVAAENPAPSGV- 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 88853865 171 qdcgtDVLDLWTLMQDsQDFSSYLSDGLHLSPKGNEFLFSHLWPL 215
Cdd:cd00229 149 -----DLVDLAALLGD-EDKSLYSPDGIHPNPAGHKLIAEALASA 187
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 17-220 4.91e-17

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: 76.21  E-value: 4.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  17 RLLLFGDSITQfsfqqgGWGASLADRLVRKCD------VLNRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFFGAND 90
Cdd:cd04501   2 RVVCLGDSITY------GYPVGPEASWVNLLAeflgkeVINRGINGDTTSQ---MLVRFYEDVIALK-PAVVIIMGGTND 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  91 SAlkdenpkQHIPLEEYAANLKSMVQYLKSVDIpenRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYanaclqvA 170
Cdd:cd04501  72 II-------VNTSLEMIKDNIRSMVELAEANGI---KVILASPLPVDDYPWKPQWLRPANKLKSLNRWLKDY-------A 134

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 88853865 171 QDCGTDVLDLWTLMQDSQDF---SSYLSDGLHLSPKGNEFLFshlwPLIEKKV 220
Cdd:cd04501 135 RENGLLFLDFYSPLLDERNVglkPGLLTDGLHPSREGYRVMA----PLAEKAL 183
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 16-204 2.13e-16

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: 74.94  E-value: 2.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  16 PRLLLFGDSITQ---FSFQQGGWGASLADRLVRKCDVLNRGFSGYNTR-------WAKIIlpRLIRKGnslDIpvaVTIF 85
Cdd:cd01821   1 PTIFLAGDSTVAdydPGAPQAGWGQALPQYLDTGITVVNHAKGGRSSRsfrdegrWDAIL--KLIKPG---DY---VLIQ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  86 FGANDSalKDENPKQHIPLEEYAANLKSMVQylksvdipENR-----VILITPTPlcETAWEEQciiqgcklNRLNSVVG 160
Cdd:cd01821  73 FGHNDQ--KPKDPEYTEPYTTYKEYLRRYIA--------EARakgatPILVTPVT--RRTFDEG--------GKVEDTLG 132

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 88853865 161 EYANACLQVAQDCGTDVLDLWTLMQD----------SQDFSSYLSDGLHLSPKG 204
Cdd:cd01821 133 DYPAAMRELAAEEGVPLIDLNAASRAlyeaigpeksKKYFPEGPGDNTHFSEKG 186
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 17-213 2.58e-15

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: 71.94  E-value: 2.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  17 RLLLFGDSITQfsfqQGGWGASLADRLV-----RKCDVLNRGFSGYNTRwakIILPRLIRKGNSLDiPVAVTIFFGANDS 91
Cdd:cd01834   3 RIVFIGNSITD----RGGYVGYVETYLAarypeLKLTFRNLGWSGDTVS---DLAARRDRDVLPAK-PDVVSIMFGINDS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  92 AlkdENPKQHIPLEEYAANLKSMVQYLKSvDIPENRVILITPTplcetaWEEQCIIQGCKLNRLNSVVGEYANACLQVAQ 171
Cdd:cd01834  75 F---RGFDDPVGLEKFKTNLRRLIDRLKN-KESAPRIVLVSPI------AYEANEDPLPDGAEYNANLAAYADAVRELAA 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 88853865 172 DCGTDVLDLWTLM---QDSQDFSSYLSDGLHLSPKGNeFLFSHLW 213
Cdd:cd01834 145 ENGVAFVDLFTPMkeaFQKAGEAVLTVDGVHPNEAGH-RALARLW 188
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 17-204 2.36e-13

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: 65.76  E-value: 2.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  17 RLLLFGDSITQFsfqqGGWGASLADRlvrkcDVLNRGFSGYNTRWakiILPRL--IRKGNsldiPVAVTIFFGANDSAlk 94
Cdd:cd01828   1 ALVFLGDSLTEG----GPWALLFPDV-----KVANRGISGDTTRG---LLARLdeDVALQ----PKAIFIMIGINDLA-- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  95 denpkQHIPLEEYAANLKSMVQYLKSVDiPENRVILITPTPLCETAWeeqciiqgcklnRLNSVVGEyANACL-QVAQDC 173
Cdd:cd01828  63 -----QGTSDEDIVANYRTILEKLRKHF-PNIKIVVQSILPVGELKS------------IPNEQIEE-LNRQLaQLAQQE 123

                       170       180       190
                ....*....|....*....|....*....|...
gi 88853865 174 GTDVLDLWTLMQDSQDFSS--YLSDGLHLSPKG 204
Cdd:cd01828 124 GVTFLDLWAVFTNADGDLKneFTTDGLHLNAKG 156
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 19-212 5.37e-09

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: 53.87  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  19 LLFGDSITQFSFQQGGWGASladrlvrkCDVLNRGFSGYNTRWA-KIILPRLIRKgnsldIPVAVTIFFGANDSALKden 97
Cdd:cd01841   4 VFIGDSLFEGWPLYEAEGKG--------KTVNNLGIAGISSRQYlEHIEPQLIQK-----NPSKVFLFLGTNDIGKE--- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  98 pkqhIPLEEYAANLKSMVQYLKSvDIPENRVILITPTPLCETAWEEQciiqgcklnRLNSVVGEYANACLQVAQDCGTDV 177
Cdd:cd01841  68 ----VSSNQFIKWYRDIIEQIRE-EFPNTKIYLLSVLPVLEEDEIKT---------RSNTRIQRLNDAIKELAPELGVTF 133

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 88853865 178 LDLWTLMQDS--QDFSSYLSDGLHLSPKGNEFLFSHL 212
Cdd:cd01841 134 IDLNDVLVDEfgNLKKEYTTDGLHFNPKGYQKLLEIL 170
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 16-217 9.67e-09

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: 53.29  E-value: 9.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  16 PRLLLFGDSITQ-FSFQQG-GWGASLADRLVRKC---DVLNRGFSGYNTRWAKIILPRLIRKGNsldiPVAVTIFFGAND 90
Cdd:cd01822   1 VTILALGDSLTAgYGLPPEeGWPALLQKRLDARGidvTVINAGVSGDTTAGGLARLPALLAQHK----PDLVILELGGND 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  91 SalkdenpKQHIPLEEYAANLKSMVQYLKSVDIPenrVIL----ITPT--PLCETAWEEQciiqgcklnrlnsvvgeYAn 164
Cdd:cd01822  77 G-------LRGIPPDQTRANLRQMIETAQARGAP---VLLvgmqAPPNygPRYTRRFAAI-----------------YP- 128

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88853865 165 aclQVAQDCGT--------DVLDLWTLMQdsqdfssylSDGLHLSPKGNEFLFSHLWPLIE 217
Cdd:cd01822 129 ---ELAEEYGVplvpffleGVAGDPELMQ---------SDGIHPNAEGQPIIAENVWPALE 177
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 49-204 2.33e-06

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: 239946  Cd Length: 171  Bit Score: 46.51  E-value: 2.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  49 VLNRGFSGYNTRWAKIILPRLIRKGNsldiPVAVTIFFGANDSAlKDENPkqhiplEEYAANLKSMVQYLKSvDIPENRV 128
Cdd:cd04502  25 VVNRGFGGSTLADCLHYFDRLVLPYQ----PRRVVLYAGDNDLA-SGRTP------EEVLRDFRELVNRIRA-KLPDTPI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865 129 ILI--TPTPLCETAWEeqciiqgcKLNRLNSVVGEYAnaclqvAQDCGTDVLDLWTLMQDSQD---FSSYLSDGLHLSPK 203
Cdd:cd04502  93 AIIsiKPSPARWALRP--------KIRRFNALLKELA------ETRPNLTYIDVASPMLDADGkprAELFQEDGLHLNDA 158


                .
gi 88853865 204 G 204
Cdd:cd04502 159 G 159
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 17-215 3.94e-06

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: 46.11  E-value: 3.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  17 RLLLFGDSITQfSFQQGGWGA---SLADRLVRKC-------DVLNRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFF 86
Cdd:cd01832   1 RYVALGDSITE-GVGDPVPDGgyrGWADRLAAALaaadpgiEYANLAVRGRRTAQ---ILAEQLPAALALR-PDLVTLLA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853865  87 GANDsALKdenPKqhIPLEEYAANLKSMVqylKSVDIPENRVILIT------PTPLCETaweeqciiQGCKLNRLNSVVG 160
Cdd:cd01832  76 GGND-ILR---PG--TDPDTYRADLEEAV---RRLRAAGARVVVFTipdpavLEPFRRR--------VRARLAAYNAVIR 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 88853865 161 EyanaclqVAQDCGTDVLDLWTL--MQDSQDFSSylsDGLHLSPKGNEFLFSHLWPL 215
Cdd:cd01832 139 A-------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.
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