NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|70887543|ref|NP_001020640|]
View 

isoamyl acetate-hydrolyzing esterase 1 homolog [Danio rerio]

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 ...
 11-209 5.41e-94

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: 273.74  E-value: 5.41e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  11 QIILFGDSITQFAFQAN--GWGSELCHKLERKCDVINRGLSGYNTRWAKIVLPRIVP-VSDAPISAVTVFFGANDCALED 87
Cdd:cd01838   1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLeEKLAQPDLVTIFFGANDAALPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  88 KNptQHVPLQEFSENLKDIVRFLVSKgVSNDNIIFITPPPLLEADWEKECLLKGSPLNRLNSVAGQYAQACVQAAGESGV 167
Cdd:cd01838  81 QP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 70887543 168 DVLDLWTLMQKDGQDFSVYLSDGLHLSDKGNQFVAEHLWTLL 209
Cdd:cd01838 158 PVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLFEEIVKVI 199
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 11-209 5.41e-94

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: 273.74  E-value: 5.41e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  11 QIILFGDSITQFAFQAN--GWGSELCHKLERKCDVINRGLSGYNTRWAKIVLPRIVP-VSDAPISAVTVFFGANDCALED 87
Cdd:cd01838   1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLeEKLAQPDLVTIFFGANDAALPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  88 KNptQHVPLQEFSENLKDIVRFLVSKgVSNDNIIFITPPPLLEADWEKECLLKGSPLNRLNSVAGQYAQACVQAAGESGV 167
Cdd:cd01838  81 QP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 70887543 168 DVLDLWTLMQKDGQDFSVYLSDGLHLSDKGNQFVAEHLWTLL 209
Cdd:cd01838 158 PVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 10-210 2.35e-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: 116.28  E-value: 2.35e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  10 PQIILFGDSITQ--FAFQANGWGSELCHKL-ERKCDVINRGLSGYNTRWakiVLPRIVP-VSDAPISAVTVFFGANDCAl 85
Cdd:COG2755   9 LRIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRdLLALKPDLVVIELGTNDLL- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  86 edknPTQHVPLQEFSENLKDIVRFLVSKGvSNDNIIFITPPPLLEAdwekecllkgsplNRLNSVAGQYAQACVQAAGES 165
Cdd:COG2755  85 ----RGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAEY 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 70887543 166 GVDVLDLWTLMQKDGQDFSVYLSDGLHLSDKGNQFVAEHLWTLLE 210
Cdd:COG2755 147 GVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
12-205 4.06e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 98.03  E-value: 4.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543    12 IILFGDSITQFAFQANG----WGSELCHKLERKCDV--------INRGLSGYNTRWAKIVLPRI------VPVSDAPiSA 73
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVpgsgynhgANFAIGGATIEDLPIQLEQLlrlisdVKDQAKP-DL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543    74 VTVFFGANDCALEDKNPTQ-----HVPLQEFSENLKDIVRFLVSKGVSNDNIIFITPPPLLEADWEKEcllKGSPLNRLN 148
Cdd:pfam00657  80 VTIFIGANDLCNFLSSPARskkrvPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNAL---AEEYNERLN 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 70887543   149 SVAGQYAQAcvqaAGESGVDVLDLWTLMQKDGQDFSVYLS-DGLHLSDKGNQFVAEHL 205
Cdd:pfam00657 157 ELVNSLAAA----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 ...
 11-209 5.41e-94

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: 273.74  E-value: 5.41e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  11 QIILFGDSITQFAFQAN--GWGSELCHKLERKCDVINRGLSGYNTRWAKIVLPRIVP-VSDAPISAVTVFFGANDCALED 87
Cdd:cd01838   1 KIVLFGDSITQFSFDQGefGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLeEKLAQPDLVTIFFGANDAALPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  88 KNptQHVPLQEFSENLKDIVRFLVSKgVSNDNIIFITPPPLLEADWEKECLLKGSPLNRLNSVAGQYAQACVQAAGESGV 167
Cdd:cd01838  81 QP--QHVPLDEYKENLRKIVSHLKSL-SPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 70887543 168 DVLDLWTLMQKDGQDFSVYLSDGLHLSDKGNQFVAEHLWTLL 209
Cdd:cd01838 158 PVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLFEEIVKVI 199
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 10-210 2.35e-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: 116.28  E-value: 2.35e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  10 PQIILFGDSITQ--FAFQANGWGSELCHKL-ERKCDVINRGLSGYNTRWakiVLPRIVP-VSDAPISAVTVFFGANDCAl 85
Cdd:COG2755   9 LRIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRdLLALKPDLVVIELGTNDLL- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  86 edknPTQHVPLQEFSENLKDIVRFLVSKGvSNDNIIFITPPPLLEAdwekecllkgsplNRLNSVAGQYAQACVQAAGES 165
Cdd:COG2755  85 ----RGLGVSPEEFRANLEALIDRLRAAG-PGARVVLVTPPPRLRP-------------NYLNERIEAYNAAIRELAAEY 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 70887543 166 GVDVLDLWTLMQKDGQDFSVYLSDGLHLSDKGNQFVAEHLWTLLE 210
Cdd:COG2755 147 GVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
12-205 4.06e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 98.03  E-value: 4.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543    12 IILFGDSITQFAFQANG----WGSELCHKLERKCDV--------INRGLSGYNTRWAKIVLPRI------VPVSDAPiSA 73
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVpgsgynhgANFAIGGATIEDLPIQLEQLlrlisdVKDQAKP-DL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543    74 VTVFFGANDCALEDKNPTQ-----HVPLQEFSENLKDIVRFLVSKGVSNDNIIFITPPPLLEADWEKEcllKGSPLNRLN 148
Cdd:pfam00657  80 VTIFIGANDLCNFLSSPARskkrvPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNAL---AEEYNERLN 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 70887543   149 SVAGQYAQAcvqaAGESGVDVLDLWTLMQKDGQDFSVYLS-DGLHLSDKGNQFVAEHL 205
Cdd:pfam00657 157 ELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 14-199 4.78e-25

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: 97.23  E-value: 4.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543    14 LFGDSITQ---FAFQANGWGSELCHKLERKCD---VINRGLSGYNTRwaKIVLPRIVPVSDAPISAVTVFFGANDCAled 87
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLARRLGadvVNNLGISGATTR--LDLLERLDDVLRLKPDLVVILLGTNDLG--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543    88 knptQHVPLQEFSENLKDIVRFLVSKGvSNDNIIFITPPPLLEADWEkecllkgsPLNRLNSVAGQYAQACVQAAGESGV 167
Cdd:pfam13472  76 ----RGVSAARAAANLEALIDALRAAG-PDARVLLIGPLPVGPPPPL--------DERRLNARIAEYNAAIREVAAERGV 142

                         170       180       190
                  ....*....|....*....|....*....|...
gi 70887543   168 DVLDLWTLMQKDGQDFSVYLS-DGLHLSDKGNQ 199
Cdd:pfam13472 143 PYVDLWDALRDDGGWLPDLLAdDGLHPNAAGYR 175
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 12-208 1.45e-20

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: 85.54  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  12 IILFGDSITQ---FAFQANGWGSELCHKLERKCD---VINRGLSGYNTRWAKIVLPRIVPVSDAPISAVTVFFGANDCAL 85
Cdd:cd00229   1 ILVIGDSITAgygASSGSTFYSLLLYLLLLAGGPgveVINLGVSGATTADALRRLGLRLALLKDKPDLVIIELGTNDLGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  86 EdknptQHVPLQEFSENLKDIVRFLVSKgVSNDNIIFITPPPLLEADWekeclLKGSPLNRLNSVAGQYAQAcvqAAGES 165
Cdd:cd00229  81 G-----GDTSIDEFKANLEELLDALRER-APGAKVILITPPPPPPREG-----LLGRALPRYNEAIKAVAAE---NPAPS 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 70887543 166 GVDVLDLWTLMQKDGQDFsvYLSDGLHLSDKGNQFVAEHLWTL 208
Cdd:cd00229 147 GVDLVDLAALLGDEDKSL--YSPDGIHPNPAGHKLIAEALASA 187
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 11-197 1.27e-15

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: 71.93  E-value: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  11 QIILFGDSITQFafqaNGWGSELCHKlerkcDVINRGLSGYNTRWakiVLPRIVPVSDAPISAVTVFFGANDCAledknp 90
Cdd:cd01828   1 ALVFLGDSLTEG----GPWALLFPDV-----KVANRGISGDTTRG---LLARLDEDVALQPKAIFIMIGINDLA------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  91 tQHVPLQEFSENLKDIVRFLvsKGVSNDNIIFI--TPP--PLLEADWEKecllkgspLNRLNSVAGQYAQacvqaagESG 166
Cdd:cd01828  63 -QGTSDEDIVANYRTILEKL--RKHFPNIKIVVqsILPvgELKSIPNEQ--------IEELNRQLAQLAQ-------QEG 124

                       170       180       190
                ....*....|....*....|....*....|..
gi 70887543 167 VDVLDLWT-LMQKDGQDFSVYLSDGLHLSDKG 197
Cdd:cd01828 125 VTFLDLWAvFTNADGDLKNEFTTDGLHLNAKG 156
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 10-205 4.33e-13

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: 65.04  E-value: 4.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  10 PQIILFGDSITQFaFQANGWgselchkLERKCDVINRGLSGYNTRWAK--IVLPRIVPVSDApisaVTVFFGANDCALEd 87
Cdd:cd01841   1 KNIVFIGDSLFEG-WPLYEA-------EGKGKTVNNLGIAGISSRQYLehIEPQLIQKNPSK----VFLFLGTNDIGKE- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  88 knptqhVPLQEFSENLKDIVRFLVSKgVSNDNIIFITPPPLLEADWEKEcllkgsplnRLNSVAGQYAQACVQAAGESGV 167
Cdd:cd01841  68 ------VSSNQFIKWYRDIIEQIREE-FPNTKIYLLSVLPVLEEDEIKT---------RSNTRIQRLNDAIKELAPELGV 131

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 70887543 168 DVLDLWT-LMQKDGQDFSVYLSDGLHLSDKGNQFVAEHL 205
Cdd:cd01841 132 TFIDLNDvLVDEFGNLKKEYTTDGLHFNPKGYQKLLEIL 170
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 10-202 2.75e-12

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: 63.39  E-value: 2.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  10 PQIILFGDSITQ---FAFQANGWGSELCHKLERKCDVINRGLSGYNTR-------WAKIvLPRIVPvsdAPIsaVTVFFG 79
Cdd:cd01821   1 PTIFLAGDSTVAdydPGAPQAGWGQALPQYLDTGITVVNHAKGGRSSRsfrdegrWDAI-LKLIKP---GDY--VLIQFG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  80 ANDCAleDKNPTQHVPLQEFSENLKDIVRFLVSKGVsndNIIFITPPPllEADWEKEcllkgsplNRLNSVAGQYAQACV 159
Cdd:cd01821  75 HNDQK--PKDPEYTEPYTTYKEYLRRYIAEARAKGA---TPILVTPVT--RRTFDEG--------GKVEDTLGDYPAAMR 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 70887543 160 QAAGESGVDVLDLWT----LMQKDGQD-----FSVYLSDGLHLSDKGNQFVA 202
Cdd:cd01821 140 ELAAEEGVPLIDLNAasraLYEAIGPEkskkyFPEGPGDNTHFSEKGADVVA 191
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 12-209 1.49e-11

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: 61.19  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  12 IILFGDSITQfafqanGWG-------SELCHKLERKcDVINRGLSGYNTRWAKIVLPRIVpVSDAPiSAVTVFFGANDCA 84
Cdd:cd04501   3 VVCLGDSITY------GYPvgpeaswVNLLAEFLGK-EVINRGINGDTTSQMLVRFYEDV-IALKP-AVVIIMGGTNDII 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  85 ledknptQHVPLQEFSENLKDIVRFLVSKGVSndnIIFITPPPLLEADWEKECLLKGSPLNRLNSVAGQYAQacvqaagE 164
Cdd:cd04501  74 -------VNTSLEMIKDNIRSMVELAEANGIK---VILASPLPVDDYPWKPQWLRPANKLKSLNRWLKDYAR-------E 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 70887543 165 SGVDVLDLWTLM--QKDGQDFSVYLSDGLHLSDKGNQFVAEHLWTLL 209
Cdd:cd04501 137 NGLLFLDFYSPLldERNVGLKPGLLTDGLHPSREGYRVMAPLAEKAL 183
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 13-206 2.25e-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: 60.77  E-value: 2.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  13 ILF-GDSITQfAFQANGWGSELCHKL--ERKCDVINRGLSGYNTrwAKIVLPRIVPVSDAPISAVTVFFGANDCAledKN 89
Cdd:cd01834   4 IVFiGNSITD-RGGYVGYVETYLAARypELKLTFRNLGWSGDTV--SDLAARRDRDVLPAKPDVVSIMFGINDSF---RG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  90 PTQHVPLQEFSENLKDIVRFLVSKGvSNDNIIFITPPPlLEADWEKECLLKGsplnrLNSVAGQYAQACVQAAGESGVDV 169
Cdd:cd01834  78 FDDPVGLEKFKTNLRRLIDRLKNKE-SAPRIVLVSPIA-YEANEDPLPDGAE-----YNANLAAYADAVRELAAENGVAF 150

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 70887543 170 LDLWTLMQK--DGQDFSVYLSDGLHLSDKGnQFVAEHLW 206
Cdd:cd01834 151 VDLFTPMKEafQKAGEAVLTVDGVHPNEAG-HRALARLW 188
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 43-197 7.96e-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: 239946  Cd Length: 171  Bit Score: 47.67  E-value: 7.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  43 VINRGLSGYNTRWAKIVLPRIVPvSDAPiSAVTVFFGANDCAlEDKNPtqhvplQEFSENLKDIVRfLVSKGVSNDNIIF 122
Cdd:cd04502  25 VVNRGFGGSTLADCLHYFDRLVL-PYQP-RRVVLYAGDNDLA-SGRTP------EEVLRDFRELVN-RIRAKLPDTPIAI 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887543 123 I--TPPPLLEADWEKecllkgspLNRLNSVAGQYAQAcvqaagESGVDVLDLWTLM-QKDGQ-DFSVYLSDGLHLSDKG 197
Cdd:cd04502  95 IsiKPSPARWALRPK--------IRRFNALLKELAET------RPNLTYIDVASPMlDADGKpRAELFQEDGLHLNDAG 159
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 12-210 2.29e-06

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: 46.35  E-value: 2.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  12 IILFGDSITQfAFQAN---GWGSELCHKLERKC---DVINRGLSGYNTRWAKIVLPRIvpVSDAPISAVTVFFGANDcAL 85
Cdd:cd01822   3 ILALGDSLTA-GYGLPpeeGWPALLQKRLDARGidvTVINAGVSGDTTAGGLARLPAL--LAQHKPDLVILELGGND-GL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  86 edknptQHVPLQEFSENLKDIVRFLVSKGVsndniifitppplleadwekECLLKGSPL--NRLNSVAGQYAQACVQAAG 163
Cdd:cd01822  79 ------RGIPPDQTRANLRQMIETAQARGA--------------------PVLLVGMQAppNYGPRYTRRFAAIYPELAE 132

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 70887543 164 ESGV--------DVLDLWTLMQkdgqdfsvylSDGLHLSDKGNQFVAEHLWTLLE 210
Cdd:cd01822 133 EYGVplvpffleGVAGDPELMQ----------SDGIHPNAEGQPIIAENVWPALE 177
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
 11-205 1.39e-05

SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating enzyme) of A. tumefaciens. 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: 238877  Cd Length: 208  Bit Score: 44.57  E-value: 1.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  11 QIILFGDSIT---------QFAFQANgWGSELCHKL---ERKCDVINRGLSGYNTRWAKIVLP-----RIVPV---SDAP 70
Cdd:cd01839   1 TILCFGDSNTwgiipdtggRYPFEDR-WPGVLEKALganGENVRVIEDGLPGRTTVLDDPFFPgrnglTYLPQaleSHSP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  71 ISAVTVFFGANDCALEDKNPTQHVplQEFSENLKDIVRFLVSKGVSND-NIIFITPPPLLEADWEKECLLKGSPLnrlns 149
Cdd:cd01839  80 LDLVIIMLGTNDLKSYFNLSAAEI--AQGLGALVDIIRTAPIEPGMPApKILIVAPPPIRTPKGSLAGKFAGAEE----- 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 70887543 150 VAGQYAQACVQAAGESGVDVLDLWTLMQKDGQDfsvylsdGLHLSDKGNQFVAEHL 205
Cdd:cd01839 153 KSKGLADAYRALAEELGCHFFDAGSVGSTSPVD-------GVHLDADQHAALGQAL 201
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 11-206 7.05e-05

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: 238873  Cd Length: 193  Bit Score: 42.32  E-value: 7.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  11 QIILFGDSitqFAF-----QANGWGSELCHKLERKCDVIN--------RGLSGYNTRWAKIVLPRIVpvSDAPiSAVTVF 77
Cdd:cd01835   3 RLIVVGDS---LVYgwgdpEGGGWVGRLRARWMNLGDDPVlynlgvrgDGSEDVAARWRAEWSRRGE--LNVP-NRLVLS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  78 FGANDCALEDKNPTQHVPlQEFSENLKDivrfLVSKGVSNDNIIFITPPPLLEADwekecllkgspLNRLNSVAGQYAQA 157
Cdd:cd01835  77 VGLNDTARGGRKRPQLSA-RAFLFGLNQ----LLEEAKRLVPVLVVGPTPVDEAK-----------MPYSNRRIARLETA 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 70887543 158 CVQAAGESGVDVLDLWTLMQKDGQDFSVYLS-DGLHLSDKGNQFVAEHLW 206
Cdd:cd01835 141 FAEVCLRRDVPFLDTFTPLLNHPQWRRELAAtDGIHPNAAGYGWLAWLVL 190
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 12-206 8.32e-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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


Pssm-ID: 238870  Cd Length: 185  Bit Score: 41.87  E-value: 8.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  12 IILFGDSITQ------FAFQANGWGSELCHKLERKCDVI---NRGLSGYNTRwaKIVLPRIVPVSDAPISAVTVFFGAND 82
Cdd:cd01832   2 YVALGDSITEgvgdpvPDGGYRGWADRLAAALAAADPGIeyaNLAVRGRRTA--QILAEQLPAALALRPDLVTLLAGGND 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  83 cALEDKnptqhVPLQEFSENLKDIVRFLVSKGVSndniIFITPPPLLEAdWEKECLLKGSPLNRLNSVAGQYAQacvqaa 162
Cdd:cd01832  80 -ILRPG-----TDPDTYRADLEEAVRRLRAAGAR----VVVFTIPDPAV-LEPFRRRVRARLAAYNAVIRAVAA------ 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 70887543 163 gESGVDVLDLWTLmqKDGQDFSVYLSDGLHLSDKGNQFVAEHLW 206
Cdd:cd01832 143 -RYGAVHVDLWEH--PEFADPRLWASDRLHPSAAGHARLAALVL 183
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 11-205 5.53e-04

SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. 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: 238874  Cd Length: 191  Bit Score: 39.56  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  11 QIILFGDSItqfafqANGWG-------------SELCHKLERKCDVINRGLSGYNTrwaKIVLPRIVPVSDAPISAVTVF 77
Cdd:cd01836   4 RLLVLGDST------AAGVGvetqdqalagqlaRGLAAITGRGVRWRLFAKTGATS---ADLLRQLAPLPETRFDVAVIS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887543  78 FGANDCaledknpTQHVPLQEFSENLKDIVRfLVSKGVSNDNIIFITPPPLLEADwekecLLKgSPLNRL-----NSVAG 152
Cdd:cd01836  75 IGVNDV-------THLTSIARWRKQLAELVD-ALRAKFPGARVVVTAVPPLGRFP-----ALP-QPLRWLlgrraRLLNR 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 70887543 153 QYAQACVQAAGesgVDVLDLWTLMQKDGqdfsvYLSDGLHLSDKGNQFVAEHL 205
Cdd:cd01836 141 ALERLASEAPR---VTLLPATGPLFPAL-----FASDGFHPSAAGYAVWAEAL 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