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Conserved domains on  [gi|15232826|ref|NP_190340|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
4-255 7.00e-31

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 115.01  E-value: 7.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   4 SQGSTQQKIVILNSHNENLVGLLH----ETGSTEIVVLCHGFRSNKnfEIMKNVAVAIEREGISAFRFDFSGNGESEGSF 79
Cdd:COG1073   5 SDKVNKEDVTFKSRDGIKLAGDLYlpagASKKYPAVVVAHGNGGVK--EQRALYAQRLAELGFNVLAFDYRGYGESEGEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  80 -YYGnyNYEADDLHSVIQYFSNL-----NRVVtiILGHSKGGDVVLLYASKYHDIPNVINLSGRYDLKKGIGERLGEDFL 153
Cdd:COG1073  83 rEEG--SPERRDARAAVDYLRTLpgvdpERIG--LLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAAQRAKEARG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 154 ERIKQQGYidvkdgdsGYRVTEESLMdrlnTDMHEACLKIDK-ECRVLTVHGSGDETVPVEDAKEFAKIIP-NHELQIVE 231
Cdd:COG1073 159 AYLPGVPY--------LPNVRLASLL----NDEFDPLAKIEKiSRPLLFIHGEKDEAVPFYMSEDLYEAAAePKELLIVP 226
                       250       260
                ....*....|....*....|....*.
gi 15232826 232 GADH--CYTNYQSQLVLTVMEFIKSH 255
Cdd:COG1073 227 GAGHvdLYDRPEEEYFDKLAEFFKKN 252
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
4-255 7.00e-31

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 115.01  E-value: 7.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   4 SQGSTQQKIVILNSHNENLVGLLH----ETGSTEIVVLCHGFRSNKnfEIMKNVAVAIEREGISAFRFDFSGNGESEGSF 79
Cdd:COG1073   5 SDKVNKEDVTFKSRDGIKLAGDLYlpagASKKYPAVVVAHGNGGVK--EQRALYAQRLAELGFNVLAFDYRGYGESEGEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  80 -YYGnyNYEADDLHSVIQYFSNL-----NRVVtiILGHSKGGDVVLLYASKYHDIPNVINLSGRYDLKKGIGERLGEDFL 153
Cdd:COG1073  83 rEEG--SPERRDARAAVDYLRTLpgvdpERIG--LLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAAQRAKEARG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 154 ERIKQQGYidvkdgdsGYRVTEESLMdrlnTDMHEACLKIDK-ECRVLTVHGSGDETVPVEDAKEFAKIIP-NHELQIVE 231
Cdd:COG1073 159 AYLPGVPY--------LPNVRLASLL----NDEFDPLAKIEKiSRPLLFIHGEKDEAVPFYMSEDLYEAAAePKELLIVP 226
                       250       260
                ....*....|....*....|....*.
gi 15232826 232 GADH--CYTNYQSQLVLTVMEFIKSH 255
Cdd:COG1073 227 GAGHvdLYDRPEEEYFDKLAEFFKKN 252
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
34-235 6.50e-11

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 60.69  E-value: 6.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826    34 IVVLCHGF--RSNKNFEIMKNVAvaieREGISAFRFDFSGNGESEGSFYY-GNYNYEADDLHSVIQYFSNLNRVV-TIIL 109
Cdd:pfam12146   6 VVVLVHGLgeHSGRYAHLADALA----AQGFAVYAYDHRGHGRSDGKRGHvPSFDDYVDDLDTFVDKIREEHPGLpLFLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   110 GHSKGGDVVLLYASKYHDIPNVINLSG---RYDLKKGI-GERLGEDFLERIKQQGYI-DVKDGDSGYRVTEEslMDRLNT 184
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSApalKIKPYLAPpILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEV--VAAYAA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232826   185 D--MHEAC--------LKIDKECR---------VLTVHGSGDETVPVEDAKEFAKIIP--NHELQIVEGADH 235
Cdd:pfam12146 160 DplVHGGIsartlyelLDAGERLLrraaaitvpLLLLHGGADRVVDPAGSREFYERAGstDKTLKLYPGLYH 231
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
4-255 7.00e-31

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 115.01  E-value: 7.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   4 SQGSTQQKIVILNSHNENLVGLLH----ETGSTEIVVLCHGFRSNKnfEIMKNVAVAIEREGISAFRFDFSGNGESEGSF 79
Cdd:COG1073   5 SDKVNKEDVTFKSRDGIKLAGDLYlpagASKKYPAVVVAHGNGGVK--EQRALYAQRLAELGFNVLAFDYRGYGESEGEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  80 -YYGnyNYEADDLHSVIQYFSNL-----NRVVtiILGHSKGGDVVLLYASKYHDIPNVINLSGRYDLKKGIGERLGEDFL 153
Cdd:COG1073  83 rEEG--SPERRDARAAVDYLRTLpgvdpERIG--LLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAAQRAKEARG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 154 ERIKQQGYidvkdgdsGYRVTEESLMdrlnTDMHEACLKIDK-ECRVLTVHGSGDETVPVEDAKEFAKIIP-NHELQIVE 231
Cdd:COG1073 159 AYLPGVPY--------LPNVRLASLL----NDEFDPLAKIEKiSRPLLFIHGEKDEAVPFYMSEDLYEAAAePKELLIVP 226
                       250       260
                ....*....|....*....|....*.
gi 15232826 232 GADH--CYTNYQSQLVLTVMEFIKSH 255
Cdd:COG1073 227 GAGHvdLYDRPEEEYFDKLAEFFKKN 252
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
34-235 3.98e-19

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 83.13  E-value: 3.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  34 IVVLCHGFRSNKnfEIMKNVAVAIEREGISAFRFDFSGNGESEGSF-YYGNYNYEADDLHSVIQYFSNLNRVVTIILGHS 112
Cdd:COG2267  30 TVVLVHGLGEHS--GRYAELAEALAAAGYAVLAFDLRGHGRSDGPRgHVDSFDDYVDDLRAALDALRARPGLPVVLLGHS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 113 KGGDVVLLYASKYHDIPN-VINLSGRYDlkkgigerlgEDFLERIKQQGYIDVKdgdsgyrvteeslmdrlntdMHEACL 191
Cdd:COG2267 108 MGGLIALLYAARYPDRVAgLVLLAPAYR----------ADPLLGPSARWLRALR--------------------LAEALA 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15232826 192 KIDkeCRVLTVHGSGDETVPVEDAKEFA-KIIPNHELQIVEGADH 235
Cdd:COG2267 158 RID--VPVLVLHGGADRVVPPEAARRLAaRLSPDVELVLLPGARH 200
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
13-254 9.50e-19

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 81.75  E-value: 9.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  13 VILNSHNENLVGLLH--ETGSTEIVVLCH------GFRSNKnfeIMKNVAVAIEREGISAFRFDFSGNGESEGSFYYGny 84
Cdd:COG2945   2 VLINGPAGRLEGRLDlpEGPPRGVALILHphplfgGTMDNK---VVYTLARALVAAGFAVLRFNFRGVGRSEGEFDEG-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  85 NYEADDLHSVIQYFSNLNRVVTIILGHSKGGDVVLLYASKYHDIPNVINLS---GRYDLkkgigerlgeDFLERIkqqgy 161
Cdd:COG2945  77 RGELDDAAAALDWLRAQNPLPLWLAGFSFGAYVALQLAMRLPEVEGLILVAppvNRYDF----------SFLAPC----- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 162 idvkdgdsgyrvteeslmdrlntdmheaclkidkECRVLTVHGSGDETVPVEDAKE-FAKIIPNHELQIVEGADHCYTNY 240
Cdd:COG2945 142 ----------------------------------PAPTLVIHGEQDEVVPPAEVLDwARPLSPPLPVVVVPGADHFFHGK 187
                       250
                ....*....|....
gi 15232826 241 QSQLVLTVMEFIKS 254
Cdd:COG2945 188 LDELKELVARYLPR 201
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-255 2.47e-18

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 81.22  E-value: 2.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  34 IVVLCHGFRSNKnFEIMKNVAVAIEREGISAFRFDFSGNGESEGSFYYGNYnyeaDDLHSVIQYFSNL-----NRVVtiI 108
Cdd:COG1506  25 VVVYVHGGPGSR-DDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEV----DDVLAAIDYLAARpyvdpDRIG--I 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 109 LGHSKGGDVVLLYASKYHDIPN-VINLSGRYDLKKGIGERlgEDFLERIKqqgyidvkdgdsGYRVTEESLMDRLNTDMH 187
Cdd:COG1506  98 YGHSYGGYMALLAAARHPDRFKaAVALAGVSDLRSYYGTT--REYTERLM------------GGPWEDPEAYAARSPLAY 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232826 188 EACLKidkeCRVLTVHGSGDETVPVEDAKEFAKII----PNHELQIVEGADHCYTNYQSQLVL-TVMEFIKSH 255
Cdd:COG1506 164 ADKLK----TPLLLIHGEADDRVPPEQAERLYEALkkagKPVELLVYPGEGHGFSGAGAPDYLeRILDFLDRH 232
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
30-255 1.08e-16

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 76.90  E-value: 1.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  30 GSTEIVVLCHGFRSNKNFeiMKNVAVAIEREGISAFRFDFSGNGESEGSFYygNYNYE--ADDLHSVIQYFSNLNRVVTI 107
Cdd:COG1647  13 GGRKGVLLLHGFTGSPAE--MRPLAEALAKAGYTVYAPRLPGHGTSPEDLL--KTTWEdwLEDVEEAYEILKAGYDKVIV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 108 IlGHSKGGDVVLLYASKYHDIPNVINLSG--RYDLKKGIGERLGEDFLERIKQQGyIDVKDGDS---GYRVTE-ESL--M 179
Cdd:COG1647  89 I-GLSMGGLLALLLAARYPDVAGLVLLSPalKIDDPSAPLLPLLKYLARSLRGIG-SDIEDPEVaeyAYDRTPlRALaeL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 180 DRLNTDMHEACLKIDkeCRVLTVHGSGDETVPVEDAKEFAKII--PNHELQIVEGADHCYTNY--QSQLVLTVMEFIKSH 255
Cdd:COG1647 167 QRLIREVRRDLPKIT--APTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHVITLDkdREEVAEEILDFLERL 244
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
35-255 8.87e-15

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 71.19  E-value: 8.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  35 VVLCHGFRSNknFEIMKNVAVAIeREGISAFRFDFSGNGESEGSfyYGNYNYE--ADDLHSVIQYFsNLNRVVtiILGHS 112
Cdd:COG0596  26 VVLLHGLPGS--SYEWRPLIPAL-AAGYRVIAPDLRGHGRSDKP--AGGYTLDdlADDLAALLDAL-GLERVV--LVGHS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826 113 KGGDVVLLYASKYHDipnvinlsgryDLKKGIgerLGEDFLERIKQQgyidVKDGDSGYRVTEESLMDRLNTDMHEACLK 192
Cdd:COG0596  98 MGGMVALELAARHPE-----------RVAGLV---LVDEVLAALAEP----LRRPGLAPEALAALLRALARTDLRERLAR 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232826 193 IDkeCRVLTVHGSGDETVPVEDAKEFAKIIPNHELQIVEGADHCYTNYQSQLVLTVM-EFIKSH 255
Cdd:COG0596 160 IT--VPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALrDFLARL 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
34-235 6.50e-11

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 60.69  E-value: 6.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826    34 IVVLCHGF--RSNKNFEIMKNVAvaieREGISAFRFDFSGNGESEGSFYY-GNYNYEADDLHSVIQYFSNLNRVV-TIIL 109
Cdd:pfam12146   6 VVVLVHGLgeHSGRYAHLADALA----AQGFAVYAYDHRGHGRSDGKRGHvPSFDDYVDDLDTFVDKIREEHPGLpLFLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   110 GHSKGGDVVLLYASKYHDIPNVINLSG---RYDLKKGI-GERLGEDFLERIKQQGYI-DVKDGDSGYRVTEEslMDRLNT 184
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSApalKIKPYLAPpILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEV--VAAYAA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232826   185 D--MHEAC--------LKIDKECR---------VLTVHGSGDETVPVEDAKEFAKIIP--NHELQIVEGADH 235
Cdd:pfam12146 160 DplVHGGIsartlyelLDAGERLLrraaaitvpLLLLHGGADRVVDPAGSREFYERAGstDKTLKLYPGLYH 231
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
35-235 1.75e-07

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 50.97  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826    35 VVLCHGFRSNKNFEImkNVAVAIEREGISAFRFDFSGNGESEGSFYYGNYNYE--ADDLHSVIQYFSNLNrvvTIILGHS 112
Cdd:pfam00561   3 VLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEK---VNLVGHS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   113 KGGDVVLLYASKYHD-IPNVINLSG-------------------------RYDLKKGIGERLGEDFLERIKQQGYIDVKD 166
Cdd:pfam00561  78 MGGLIALAYAAKYPDrVKALVLLGAldppheldeadrfilalfpgffdgfVADFAPNPLGRLVAKLLALLLLRLRLLKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   167 GD------SGYRVTEESL-------MDRLNT-DMHEACLKIDKecRVLTVHGSGDETVPVEDAKEFAKIIPNHELQIVEG 232
Cdd:pfam00561 158 PLlnkrfpSGDYALAKSLvtgallfIETWSTeLRAKFLGRLDE--PTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPD 235

                  ...
gi 15232826   233 ADH 235
Cdd:pfam00561 236 AGH 238
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
35-131 4.73e-04

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 38.66  E-value: 4.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826  35 VVLCHGFRSNKNfeIMKNVAVAIEREGISAFRFDFSGNGES-EGSfyygnynyeADDLHSVIQ---YFSNLNRVVtiILG 110
Cdd:COG1075   8 VVLVHGLGGSAA--SWAPLAPRLRAAGYPVYALNYPSTNGSiEDS---------AEQLAAFVDavlAATGAEKVD--LVG 74
                        90       100
                ....*....|....*....|.
gi 15232826 111 HSKGGDVVLLYASKYHDIPNV 131
Cdd:COG1075  75 HSMGGLVARYYLKRLGGAAKV 95
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
108-236 7.01e-04

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 39.96  E-value: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232826   108 ILGHSKGGDVVLLYASKYHDIPNVINLSG---------RYdlKKGIGERLGEDfLERIKQQgyidvkdgDSGYRVTEESL 178
Cdd:pfam08840  26 LLGISKGGELALSMATFLKQITATVSINGsavvsgdplVY--KDNPLPPLGEG-MRRIKVN--------KDGLLDIRDMF 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232826   179 MDRLNTDMHEACLKIDK-ECRVLTVHGSGDETVPvedAKEFAKIIP--------NHELQIV--EGADHC 236
Cdd:pfam08840  95 NDPLSKPDPKSLIPVERaKGPFLFVVGQDDHNWP---SVFYAKKACerlqkhgkEVEVQLVcyPGAGHL 160
 
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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