NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1003701409|ref|NP_001307787|]
View 

isoamyl acetate-hydrolyzing esterase 1 homolog isoform b [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2-191 1.01e-87

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: 257.18  E-value: 1.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   2 QFSFQQG--GWGASLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGnSLDIPVAVTIFFGANDSALKDENpkQHIPL 79
Cdd:cd01838    11 QFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEE-KLAQPDLVTIFFGANDAALPGQP--QHVPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  80 EEYAANLKSMVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLM 159
Cdd:cd01838    88 DEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAM 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1003701409 160 QDSQD-FSSYLSDGLHLSPKGNEFLFSHLWPLI 191
Cdd:cd01838   167 QEEAGwLESLLTDGLHFSSKGYELLFEEIVKVI 199
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 2-191 1.01e-87

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: 257.18  E-value: 1.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   2 QFSFQQG--GWGASLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGnSLDIPVAVTIFFGANDSALKDENpkQHIPL 79
Cdd:cd01838    11 QFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEE-KLAQPDLVTIFFGANDAALPGQP--QHVPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  80 EEYAANLKSMVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLM 159
Cdd:cd01838    88 DEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAM 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1003701409 160 QDSQD-FSSYLSDGLHLSPKGNEFLFSHLWPLI 191
Cdd:cd01838   167 QEEAGwLESLLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 7-192 2.28e-27

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: 103.19  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   7 QGGWGASLADRL-VRKCDVLNRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFFGANDSAlkdenPKQHIPLEEYAAN 85
Cdd:COG2755    27 ERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLALK-PDLVVIELGTNDLL-----RGLGVSPEEFRAN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  86 LKSMVQYLKSVDiPENRVILITPTPLCETaweeqciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQDF 165
Cdd:COG2755    98 LEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAEYGVPLVDLYAALRDAGDL 163

                         170       180
                  ....*....|....*....|....*...
gi 1003701409 166 SSYLS-DGLHLSPKGNEFLFSHLWPLIE 192
Cdd:COG2755   164 PDLLTaDGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
4-187 1.82e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 98.80  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   4 SFQQGGWGASLADRLVRKCDVLNrgfSGYNTRWAKII--------------LPRLIRKGNSLDIPVAVTIFFGAND--SA 67
Cdd:pfam00657  16 PGGRFSWGDLLADFLARKLGVPG---SGYNHGANFAIggatiedlpiqleqLLRLISDVKDQAKPDLVTIFIGANDlcNF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  68 LKDENPK---QHIPLEEYAANLKSMVQYLKSVDIPENRVILITPTPLCETAWEEqciIQGCKLNRLNSVVGEYANAclqv 144
Cdd:pfam00657  93 LSSPARSkkrVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNA---LAEEYNERLNELVNSLAAA---- 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1003701409 145 AQDCGTDVLDLWTLMQDSQDFSSY--LSDGLHLSPKGNEFLFSHL 187
Cdd:pfam00657 166 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 ...
 2-191 1.01e-87

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: 257.18  E-value: 1.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   2 QFSFQQG--GWGASLADRLVRKCDVLNRGFSGYNTRWAKIILPRLIRKGnSLDIPVAVTIFFGANDSALKDENpkQHIPL 79
Cdd:cd01838    11 QFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEE-KLAQPDLVTIFFGANDAALPGQP--QHVPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  80 EEYAANLKSMVQYLKSVdIPENRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLM 159
Cdd:cd01838    88 DEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAM 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1003701409 160 QDSQD-FSSYLSDGLHLSPKGNEFLFSHLWPLI 191
Cdd:cd01838   167 QEEAGwLESLLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 7-192 2.28e-27

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: 103.19  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   7 QGGWGASLADRL-VRKCDVLNRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFFGANDSAlkdenPKQHIPLEEYAAN 85
Cdd:COG2755    27 ERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLALK-PDLVVIELGTNDLL-----RGLGVSPEEFRAN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  86 LKSMVQYLKSVDiPENRVILITPTPLCETaweeqciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDSQDF 165
Cdd:COG2755    98 LEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAEYGVPLVDLYAALRDAGDL 163

                         170       180
                  ....*....|....*....|....*...
gi 1003701409 166 SSYLS-DGLHLSPKGNEFLFSHLWPLIE 192
Cdd:COG2755   164 PDLLTaDGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
4-187 1.82e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 98.80  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   4 SFQQGGWGASLADRLVRKCDVLNrgfSGYNTRWAKII--------------LPRLIRKGNSLDIPVAVTIFFGAND--SA 67
Cdd:pfam00657  16 PGGRFSWGDLLADFLARKLGVPG---SGYNHGANFAIggatiedlpiqleqLLRLISDVKDQAKPDLVTIFIGANDlcNF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  68 LKDENPK---QHIPLEEYAANLKSMVQYLKSVDIPENRVILITPTPLCETAWEEqciIQGCKLNRLNSVVGEYANAclqv 144
Cdd:pfam00657  93 LSSPARSkkrVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNA---LAEEYNERLNELVNSLAAA---- 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1003701409 145 AQDCGTDVLDLWTLMQDSQDFSSY--LSDGLHLSPKGNEFLFSHL 187
Cdd:pfam00657 166 AEDANVVYVDIYGFEDPTDPCCGIglEPDGLHPSEKGYKAVAEAI 210
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 4-181 2.75e-22

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: 89.53  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   4 SFQQGGWGASLADRLVRKCD---VLNRGFSGYNTRwakIILPRLIRKGNSLDiPVAVTIFFGANDSAlkdenpkQHIPLE 80
Cdd:pfam13472  13 TGGDRSYPGWLARLLARRLGadvVNNLGISGATTR---LDLLERLDDVLRLK-PDLVVILLGTNDLG-------RGVSAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  81 EYAANLKSMVQYLKSVDiPENRVILITPTPLCETAWEEQciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQ 160
Cdd:pfam13472  82 RAAANLEALIDALRAAG-PDARVLLIGPLPVGPPPPLDE--------RRLNARIAEYNAAIREVAAERGVPYVDLWDALR 152

                         170       180
                  ....*....|....*....|...
gi 1003701409 161 DSQD--FSSYLSDGLHLSPKGNE 181
Cdd:pfam13472 153 DDGGwlPDLLADDGLHPNAAGYR 175
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 7-179 3.19e-14

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: 68.39  E-value: 3.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   7 QGGWGASLADRLVRKCDVLNRGFSGYNTR-------WAKIIlpRLIRKGnslDIpvaVTIFFGANDSalKDENPKQHIPL 79
Cdd:cd01821    20 QAGWGQALPQYLDTGITVVNHAKGGRSSRsfrdegrWDAIL--KLIKPG---DY---VLIQFGHNDQ--KPKDPEYTEPY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  80 EEYAANLKSMVQylksvdipENR-----VILITPTPlcETAWEEQciiqgcklNRLNSVVGEYANACLQVAQDCGTDVLD 154
Cdd:cd01821    90 TTYKEYLRRYIA--------EARakgatPILVTPVT--RRTFDEG--------GKVEDTLGDYPAAMRELAAEEGVPLID 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1003701409 155 LWTLMQD----------SQDFSSYLSDGLHLSPKG 179
Cdd:cd01821   152 LNAASRAlyeaigpeksKKYFPEGPGDNTHFSEKG 186
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 24-190 7.19e-14

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: 67.44  E-value: 7.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  24 VLNRGFSGYNTRWAKIIL-PRLIRKGNSLDIpvaVTIFFGANDSALKdenpkQHIPLEEYAANLKSMVQYLKSVDiPENR 102
Cdd:cd00229    38 VINLGVSGATTADALRRLgLRLALLKDKPDL---VIIELGTNDLGRG-----GDTSIDEFKANLEELLDALRERA-PGAK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409 103 VILITPTPLceTAWEEQCIIQGCKLNRLNSVVGEYANACLQVaqdcgtDVLDLWTLMQDsQDFSSYLSDGLHLSPKGNEF 182
Cdd:cd00229   109 VILITPPPP--PPREGLLGRALPRYNEAIKAVAAENPAPSGV------DLVDLAALLGD-EDKSLYSPDGIHPNPAGHKL 179


                  ....*...
gi 1003701409 183 LFSHLWPL 190
Cdd:cd00229   180 IAEALASA 187
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 9-195 9.37e-14

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: 66.97  E-value: 9.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   9 GWGASLADRLVRKCD------VLNRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFFGANDSAlkdenpkQHIPLEEY 82
Cdd:cd04501    13 GYPVGPEASWVNLLAeflgkeVINRGINGDTTSQ---MLVRFYEDVIALK-PAVVIIMGGTNDII-------VNTSLEMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  83 AANLKSMVQYLKSVDIpenRVILITPTPLCETAWEEQCIIQGCKLNRLNSVVGEYanaclqvAQDCGTDVLDLWTLMQDS 162
Cdd:cd04501    82 KDNIRSMVELAEANGI---KVILASPLPVDDYPWKPQWLRPANKLKSLNRWLKDY-------ARENGLLFLDFYSPLLDE 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1003701409 163 QDF---SSYLSDGLHLSPKGNEFLFshlwPLIEKKV 195
Cdd:cd04501   152 RNVglkPGLLTDGLHPSREGYRVMA----PLAEKAL 183
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 23-188 7.80e-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: 61.93  E-value: 7.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  23 DVLNRGFSGYNTRwakIILPRLIRKGNSLDiPVAVTIFFGANDSAlkdENPKQHIPLEEYAANLKSMVQYLKSvDIPENR 102
Cdd:cd01834    35 TFRNLGWSGDTVS---DLAARRDRDVLPAK-PDVVSIMFGINDSF---RGFDDPVGLEKFKTNLRRLIDRLKN-KESAPR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409 103 VILITPTplcetaWEEQCIIQGCKLNRLNSVVGEYANACLQVAQDCGTDVLDLWTLM---QDSQDFSSYLSDGLHLSPKG 179
Cdd:cd01834   107 IVLVSPI------AYEANEDPLPDGAEYNANLAAYADAVRELAAENGVAFVDLFTPMkeaFQKAGEAVLTVDGVHPNEAG 180


                  ....*....
gi 1003701409 180 NeFLFSHLW 188
Cdd:cd01834   181 H-RALARLW 188
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 6-179 1.55e-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: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   6 QQGGWGASLADRlvrkcDVLNRGFSGYNTRWakiILPRL--IRKGNsldiPVAVTIFFGANDSAlkdenpkQHIPLEEYA 83
Cdd:cd01828    11 EGGPWALLFPDV-----KVANRGISGDTTRG---LLARLdeDVALQ----PKAIFIMIGINDLA-------QGTSDEDIV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  84 ANLKSMVQYLKSVDiPENRVILITPTPLCETAWeeqciiqgcklnRLNSVVGEyANACL-QVAQDCGTDVLDLWTLMQDS 162
Cdd:cd01828    72 ANYRTILEKLRKHF-PNIKIVVQSILPVGELKS------------IPNEQIEE-LNRQLaQLAQQEGVTFLDLWAVFTNA 137

                         170
                  ....*....|....*....
gi 1003701409 163 QDFSS--YLSDGLHLSPKG 179
Cdd:cd01828   138 DGDLKneFTTDGLHLNAKG 156
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 11-187 2.01e-07

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: 49.25  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  11 GASLADRL------VRKCDVLNRGFSGYNTRWA-KIILPRLIRKgnsldIPVAVTIFFGANDSALKdenpkqhIPLEEYA 83
Cdd:cd01841     7 GDSLFEGWplyeaeGKGKTVNNLGIAGISSRQYlEHIEPQLIQK-----NPSKVFLFLGTNDIGKE-------VSSNQFI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  84 ANLKSMVQYLKSvDIPENRVILITPTPLCETAWEEQciiqgcklnRLNSVVGEYANACLQVAQDCGTDVLDLWTLMQDS- 162
Cdd:cd01841    75 KWYRDIIEQIRE-EFPNTKIYLLSVLPVLEEDEIKT---------RSNTRIQRLNDAIKELAPELGVTFIDLNDVLVDEf 144

                         170       180
                  ....*....|....*....|....*.
gi 1003701409 163 -QDFSSYLSDGLHLSPKGNEFLFSHL 187
Cdd:cd01841   145 gNLKKEYTTDGLHFNPKGYQKLLEIL 170
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 24-179 2.01e-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: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  24 VLNRGFSGYNTRWAKIILPRLIRKGNsldiPVAVTIFFGANDSAlKDENPkqhiplEEYAANLKSMVQYLKSvDIPENRV 103
Cdd:cd04502    25 VVNRGFGGSTLADCLHYFDRLVLPYQ----PRRVVLYAGDNDLA-SGRTP------EEVLRDFRELVNRIRA-KLPDTPI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409 104 ILI--TPTPLCETAWEeqciiqgcKLNRLNSVVGEYAnaclqvAQDCGTDVLDLWTLMQDSQD---FSSYLSDGLHLSPK 178
Cdd:cd04502    93 AIIsiKPSPARWALRP--------KIRRFNALLKELA------ETRPNLTYIDVASPMLDADGkprAELFQEDGLHLNDA 158


                  .
gi 1003701409 179 G 179
Cdd:cd04502   159 G 159
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 6-192 3.64e-05

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: 42.89  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   6 QQGGWGASLADRLVRKC---DVLNRGFSGYNTRWAKIILPRLIRKGNsldiPVAVTIFFGANDSalkdenpKQHIPLEEY 82
Cdd:cd01822    18 PEEGWPALLQKRLDARGidvTVINAGVSGDTTAGGLARLPALLAQHK----PDLVILELGGNDG-------LRGIPPDQT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  83 AANLKSMVQYLKSVDIPenrVIL----ITPT--PLCETAWEEQciiqgcklnrlnsvvgeYAnaclQVAQDCGT------ 150
Cdd:cd01822    87 RANLRQMIETAQARGAP---VLLvgmqAPPNygPRYTRRFAAI-----------------YP----ELAEEYGVplvpff 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1003701409 151 --DVLDLWTLMQdsqdfssylSDGLHLSPKGNEFLFSHLWPLIE 192
Cdd:cd01822   143 leGVAGDPELMQ---------SDGIHPNAEGQPIIAENVWPALE 177
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 9-190 3.37e-04

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: 39.94  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409   9 GWGASLADRLVRKCDVL---NRGFSGYNTRWakiILPRLIRKGNSLDiPVAVTIFFGANDsALKdenPKqhIPLEEYAAN 85
Cdd:cd01832    24 GWADRLAAALAAADPGIeyaNLAVRGRRTAQ---ILAEQLPAALALR-PDLVTLLAGGND-ILR---PG--TDPDTYRAD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701409  86 LKSMVqylKSVDIPENRVILIT------PTPLCETaweeqciiQGCKLNRLNSVVGEyanaclqVAQDCGTDVLDLWTL- 158
Cdd:cd01832    94 LEEAV---RRLRAAGARVVVFTipdpavLEPFRRR--------VRARLAAYNAVIRA-------VAARYGAVHVDLWEHp 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1003701409 159 -MQDSQDFSSylsDGLHLSPKGNEFLFSHLWPL 190
Cdd:cd01832   156 eFADPRLWAS---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