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Conserved domains on  [gi|21700821|gb|AAM70534|]
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AT5g62930/MQB2_230 [Arabidopsis thaliana]

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 ...
 5-207 7.91e-104

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: 298.78  E-value: 7.91e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSITAQSF--RSGGWGSALADAYSRKADVVVRGYGGYNTRWALFLLHHIFPLGSSSPPVATTIFFGANDAALKGR 82
Cdd:cd01838   2 IVLFGDSITQFSFdqGEFGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEKLAQPDLVTIFFGANDAALPGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  83 TsdrQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAGRQSYAesiygEKAMKEPERTNETTGVYAQHCVALAE 162
Cdd:cd01838  82 P---QHVPLDEYKENLRKIVSHLKSLSPKTKVILITPPPVDEEAWEKSL-----EDGGSQPGRTNELLKQYAEACVEVAE 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21700821 163 ELGLRCVNLWSKMQETNDWQKKYLSDGLHLTPEGNGVVFDEVSRV 207
Cdd:cd01838 154 ELGVPVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLFEEIVKV 198
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 5-207 7.91e-104

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: 298.78  E-value: 7.91e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSITAQSF--RSGGWGSALADAYSRKADVVVRGYGGYNTRWALFLLHHIFPLGSSSPPVATTIFFGANDAALKGR 82
Cdd:cd01838   2 IVLFGDSITQFSFdqGEFGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEKLAQPDLVTIFFGANDAALPGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  83 TsdrQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAGRQSYAesiygEKAMKEPERTNETTGVYAQHCVALAE 162
Cdd:cd01838  82 P---QHVPLDEYKENLRKIVSHLKSLSPKTKVILITPPPVDEEAWEKSL-----EDGGSQPGRTNELLKQYAEACVEVAE 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21700821 163 ELGLRCVNLWSKMQETNDWQKKYLSDGLHLTPEGNGVVFDEVSRV 207
Cdd:cd01838 154 ELGVPVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLFEEIVKV 198
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
5-204 3.87e-35

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 124.22  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821     5 IVLFGDSITAQSFRSGG----WGSALADAYSRKADVVVRGYG-GYN-------TRWALFLLHHIFPLGSSS----PPVAT 68
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPGSGYNhGANfaiggatIEDLPIQLEQLLRLISDVkdqaKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821    69 TIFFGANDA----ALKGRTSDRQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAGRQSYAESIYgekamkePE 144
Cdd:pfam00657  81 TIFIGANDLcnflSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNALAEEY-------NE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21700821   145 RTNETTGVYAQHcvalAEELGLRCVNLWSKMQETNDWQKKYLS-DGLHLTPEGNGVVFDEV 204
Cdd:pfam00657 154 RLNELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 1-209 1.07e-29

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: 109.73  E-value: 1.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   1 MRPE------IVLFGDSITA--QSFRSGGWGSALADAY-SRKADVVVRGYGGYNTRWalfLLHHIFPLGSSSPPVATTIF 71
Cdd:COG2755   1 MKAAagkplrIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLALKPDLVVIE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  72 FGANDAAlkgrtsDRQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEagrqsyaesiygekamkePERTNETTG 151
Cdd:COG2755  78 LGTNDLL------RGLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLR------------------PNYLNERIE 133

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21700821 152 VYAQHCVALAEELGLRCVNLWSKMQETNDWQKKYLSDGLHLTPEGNGVVFDEVSRVFR 209
Cdd:COG2755 134 AYNAAIRELAAEYGVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 5-207 7.91e-104

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: 298.78  E-value: 7.91e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSITAQSF--RSGGWGSALADAYSRKADVVVRGYGGYNTRWALFLLHHIFPLGSSSPPVATTIFFGANDAALKGR 82
Cdd:cd01838   2 IVLFGDSITQFSFdqGEFGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEKLAQPDLVTIFFGANDAALPGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  83 TsdrQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAGRQSYAesiygEKAMKEPERTNETTGVYAQHCVALAE 162
Cdd:cd01838  82 P---QHVPLDEYKENLRKIVSHLKSLSPKTKVILITPPPVDEEAWEKSL-----EDGGSQPGRTNELLKQYAEACVEVAE 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21700821 163 ELGLRCVNLWSKMQETNDWQKKYLSDGLHLTPEGNGVVFDEVSRV 207
Cdd:cd01838 154 ELGVPVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLFEEIVKV 198
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
5-204 3.87e-35

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 124.22  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821     5 IVLFGDSITAQSFRSGG----WGSALADAYSRKADVVVRGYG-GYN-------TRWALFLLHHIFPLGSSS----PPVAT 68
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGgrfsWGDLLADFLARKLGVPGSGYNhGANfaiggatIEDLPIQLEQLLRLISDVkdqaKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821    69 TIFFGANDA----ALKGRTSDRQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAGRQSYAESIYgekamkePE 144
Cdd:pfam00657  81 TIFIGANDLcnflSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNALAEEY-------NE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21700821   145 RTNETTGVYAQHcvalAEELGLRCVNLWSKMQETNDWQKKYLS-DGLHLTPEGNGVVFDEV 204
Cdd:pfam00657 154 RLNELVNSLAAA----AEDANVVYVDIYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 1-209 1.07e-29

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: 109.73  E-value: 1.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   1 MRPE------IVLFGDSITA--QSFRSGGWGSALADAY-SRKADVVVRGYGGYNTRWalfLLHHIFPLGSSSPPVATTIF 71
Cdd:COG2755   1 MKAAagkplrIVALGDSITAgyGASRERGWPALLARRLaAADVRVVNAGISGATTAD---LLARLDRDLLALKPDLVVIE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  72 FGANDAAlkgrtsDRQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEagrqsyaesiygekamkePERTNETTG 151
Cdd:COG2755  78 LGTNDLL------RGLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLR------------------PNYLNERIE 133

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21700821 152 VYAQHCVALAEELGLRCVNLWSKMQETNDWQKKYLSDGLHLTPEGNGVVFDEVSRVFR 209
Cdd:COG2755 134 AYNAAIRELAAEYGVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 7-197 5.30e-24

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: 94.53  E-value: 5.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821     7 LFGDSITA---QSFRSGGWGSALADAYSRKAD---VVVRGYGGYNTRwalFLLHHIFPLGSSSPPVATTIFFGANDAAlk 80
Cdd:pfam13472   1 ALGDSITAgygATGGDRSYPGWLARLLARRLGadvVNNLGISGATTR---LDLLERLDDVLRLKPDLVVILLGTNDLG-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821    81 grtsdrQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIdeagrqsyaesiyGEKAMKEPERTNETTGVYAQHCVAL 160
Cdd:pfam13472  76 ------RGVSAARAAANLEALIDALRAAGPDARVLLIGPLPV-------------GPPPPLDERRLNARIAEYNAAIREV 136

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 21700821   161 AEELGLRCVNLWSKMQETNDWQKKYLS-DGLHLTPEGN 197
Cdd:pfam13472 137 AAERGVPYVDLWDALRDDGGWLPDLLAdDGLHPNAAGY 174
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 5-207 4.29e-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: 4.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSITA------QSFRSGGWGSALADAYSRKADVVVRGYGGYNTRWALFLLHHIFPLGSSSPPVATtIFFGANDAA 78
Cdd:cd00229   1 ILVIGDSITAgygassGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADALRRLGLRLALLKDKPDLVI-IELGTNDLG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  79 lkgrtsDRQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAGRQSyaesiygekaMKEPERTNEttgVYAQHCV 158
Cdd:cd00229  80 ------RGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLL----------GRALPRYNE---AIKAVAA 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21700821 159 ALAEELGLRCVNLWSKMQETNDWqkKYLSDGLHLTPEGNGVVFDEVSRV 207
Cdd:cd00229 141 ENPAPSGVDLVDLAALLGDEDKS--LYSPDGIHPNPAGHKLIAEALASA 187
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 5-211 2.63e-14

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: 68.86  E-value: 2.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSITAQsfrsGGWGSALADAYSRKA---DVVVR--GYGGYNTRwalFLLHHIFPLGSSSPPVATTIFFGANDAal 79
Cdd:cd01834   4 IVFIGNSITDR----GGYVGYVETYLAARYpelKLTFRnlGWSGDTVS---DLAARRDRDVLPAKPDVVSIMFGINDS-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  80 kGRTSDRQHVPvEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAGRQSYAESIYgEKAMKEpertnettgvYAQHCVA 159
Cdd:cd01834  75 -FRGFDDPVGL-EKFKTNLRRLIDRLKNKESAPRIVLVSPIAYEANEDPLPDGAEY-NANLAA----------YADAVRE 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21700821 160 LAEELGLRCVNLWSKMqetNDWQKK-----YLSDGLHLTPEGNGVvfdeVSRVFREA 211
Cdd:cd01834 142 LAAENGVAFVDLFTPM---KEAFQKageavLTVDGVHPNEAGHRA----LARLWLEA 191
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 4-196 7.34e-12

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: 61.91  E-value: 7.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   4 EIVLFGDSITAqsfrSGGWGSALADAysrkaDVVVRGYGGYNTRWALFLLhhifPLGSSSPPVATTIFFGANDAAlkgrt 83
Cdd:cd01828   1 ALVFLGDSLTE----GGPWALLFPDV-----KVANRGISGDTTRGLLARL----DEDVALQPKAIFIMIGINDLA----- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  84 sdrQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEaGRQSYAESIygekamkepERTNettgvyaQHCVALAEE 163
Cdd:cd01828  63 ---QGTSDEDIVANYRTILEKLRKHFPNIKIVVQSILPVGE-LKSIPNEQI---------EELN-------RQLAQLAQQ 122

                       170       180       190
                ....*....|....*....|....*....|....
gi 21700821 164 LGLRCVNLWSKM-QETNDWQKKYLSDGLHLTPEG 196
Cdd:cd01828 123 EGVTFLDLWAVFtNADGDLKNEFTTDGLHLNAKG 156
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 3-200 5.05e-10

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: 56.95  E-value: 5.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   3 PEIVLFGDSITaqsfrsGGWGsaLADAYSRKADVVVRGYGGYNTRWAL--FLLHHIFPLGSSsppvaTTIFFGANDAALK 80
Cdd:cd01841   1 KNIVFIGDSLF------EGWP--LYEAEGKGKTVNNLGIAGISSRQYLehIEPQLIQKNPSK-----VFLFLGTNDIGKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  81 grtsdrqhVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAgrqsyaesiygekaMKEPERTNETTGVYAQHCVAL 160
Cdd:cd01841  68 --------VSSNQFIKWYRDIIEQIREEFPNTKIYLLSVLPVLEE--------------DEIKTRSNTRIQRLNDAIKEL 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21700821 161 AEELGLRCVNLWSKMQETN-DWQKKYLSDGLHLTPEGNGVV 200
Cdd:cd01841 126 APELGVTFIDLNDVLVDEFgNLKKEYTTDGLHFNPKGYQKL 166
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 3-196 1.31e-09

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: 56.07  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   3 PEIVLFGDSITAQ---SFRSGGWGSALADAYSRKADVVVRGYGGYNTR-------WALfLLHHIfplgssSPPVATTIFF 72
Cdd:cd01821   1 PTIFLAGDSTVADydpGAPQAGWGQALPQYLDTGITVVNHAKGGRSSRsfrdegrWDA-ILKLI------KPGDYVLIQF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  73 GANDAalkGRTSDRQHVPVEEYTDNVRKIVQ--HLKKCSPtmliVLITPPPideagRQSYAESiygekamkepERTNETT 150
Cdd:cd01821  74 GHNDQ---KPKDPEYTEPYTTYKEYLRRYIAeaRAKGATP----ILVTPVT-----RRTFDEG----------GKVEDTL 131

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21700821 151 GVYAQHCVALAEELGLRCVNLWSKM---------QETNDWQKKYLSDGLHLTPEG 196
Cdd:cd01821 132 GDYPAAMRELAAEEGVPLIDLNAASralyeaigpEKSKKYFPEGPGDNTHFSEKG 186
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 4-208 5.36e-09

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: 54.26  E-value: 5.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   4 EIVLFGDSITAqsfrsgGWG-------SALADAYSRKaDVVVRGYGGYNTRWALFLLHHIFplgSSSPPVATTIFFGAND 76
Cdd:cd04501   2 RVVCLGDSITY------GYPvgpeaswVNLLAEFLGK-EVINRGINGDTTSQMLVRFYEDV---IALKPAVVIIMGGTND 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  77 AAlkgrtsdrQHVPVEEYTDNVRKIVQ-----HLKkcsptmlIVLITPPPIDEagrqsYAESIYGEKAMKEPERTNETTG 151
Cdd:cd04501  72 II--------VNTSLEMIKDNIRSMVElaeanGIK-------VILASPLPVDD-----YPWKPQWLRPANKLKSLNRWLK 131

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21700821 152 VYAQhcvalaeELGLRCVNLWSKM-QETNDWQKK-YLSDGLHLTPEGNGVVFDEVSRVF 208
Cdd:cd04501 132 DYAR-------ENGLLFLDFYSPLlDERNVGLKPgLLTDGLHPSREGYRVMAPLAEKAL 183
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 5-196 1.41e-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: 49.98  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSitaqSFRSggWGSALADAYSRKadVVVRGYGGYNTRWALFLLHHIFPlgsSSPPVATTIFFGANDAAlKGRTs 84
Cdd:cd04502   2 ILFYGSS----SIRL--WDTLADDLAPLP--VVNRGFGGSTLADCLHYFDRLVL---PYQPRRVVLYAGDNDLA-SGRT- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  85 drqhvpVEEYTDNVRKIVQHLKKCSPTMLIVLItpppideagrqSYAESIYGEKAMKEPERTNETTGVYAQHcvalaeEL 164
Cdd:cd04502  69 ------PEEVLRDFRELVNRIRAKLPDTPIAII-----------SIKPSPARWALRPKIRRFNALLKELAET------RP 125

                       170       180       190
                ....*....|....*....|....*....|....
gi 21700821 165 GLRCVNLWSKMQETNDWQKK--YLSDGLHLTPEG 196
Cdd:cd04502 126 NLTYIDVASPMLDADGKPRAelFQEDGLHLNDAG 159
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 5-196 9.82e-06

SGNH_peri1; putative periplasmic member of the SGNH-family of 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: 238863  Cd Length: 189  Bit Score: 44.96  E-value: 9.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSITAQSFRSGGWGSALADAYSrkaDVVVRGYGG--YNtRWALFLLHHIFplgSSSPPVATTIFFGANDAAlkgr 82
Cdd:cd01825   2 IAQLGDSHIAGDFFTDVLRGLLGVIYD---NLGVNGASAslLL-KWDAEFLQAQL---AALPPDLVILSYGTNEAF---- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  83 tsdRQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPPPIDEAgrqsyaesiYGEKAMKEPERTNEttgVYAQHcVALAE 162
Cdd:cd01825  71 ---NKQLNASEYRQQLREFIKRLRQILPNASILLVGPPDSLQK---------TGAGRWRTPPGLDA---VIAAQ-RRVAK 134

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21700821 163 ELGLRCVNLWSKMQE----TNDWQKKYLS-DGLHLTPEG 196
Cdd:cd01825 135 EEGIAFWDLYAAMGGeggiWQWAEPGLARkDYVHLTPRG 173
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 5-196 3.23e-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: 43.41  E-value: 3.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821   5 IVLFGDSIT--------AQSFRsgGWGSALADAYSRKADVV------VRGYggyntrwalfLLHHIfpLGSSSPPVAT-- 68
Cdd:cd01832   2 YVALGDSITegvgdpvpDGGYR--GWADRLAAALAAADPGIeyanlaVRGR----------RTAQI--LAEQLPAALAlr 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21700821  69 ----TIFFGANDAaLKGRTsdrqhvPVEEYTDNVRKIVQHLKKcsPTMLIVLITPPpiDEAGRQSYAESIYGEKAMkepe 144
Cdd:cd01832  68 pdlvTLLAGGNDI-LRPGT------DPDTYRADLEEAVRRLRA--AGARVVVFTIP--DPAVLEPFRRRVRARLAA---- 132

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21700821 145 rtnettgvYAQHCVALAEELGLRCVNLW--SKMQETNDWQkkylSDGLHLTPEG 196
Cdd:cd01832 133 --------YNAVIRAVAARYGAVHVDLWehPEFADPRLWA----SDRLHPSAAG 174
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
 69-120 1.38e-03

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases 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.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 39.25  E-value: 1.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21700821  69 TIFFGANDaaLKGRTSDRQHVPVEEYTDNVRKIVQHLKKCSPTMLIVLITPP 120
Cdd:cd01824 124 TIFIGGND--LCSLCEDANPGSPQTFVKNLRKALDILRDEVPRAFVNLVGLL 173
 
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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