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Conserved domains on  [gi|1063731405|ref|NP_001332157|]
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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
PubMed:  19508187|12369917|37582413

Graphical summary

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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]; ...
 37-285 1.47e-26

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 105.00  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  37 IQHQRVVIENSHGEKLVGVLH----DTGSTETVVICHGFRSSKNRipMLTIASFFERAMISSFRFDFAGNGESQGSF-QY 111
Cdd:COG1073     8 VNKEDVTFKSRDGIKLAGDLYlpagASKKYPAVVVAHGNGGVKEQ--RALYAQRLAELGFNVLAFDYRGYGESEGEPrEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 112 GNYRRevEDLRSVLQHLR---GVNRVISAIIGHSKGGNVVLLYAAKYNDVQTVVNISGrfFLDRGiefRLGKDYFKRIKD 188
Cdd:COG1073    86 GSPER--RDARAAVDYLRtlpGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSP--FTSLE---DLAAQRAKEARG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 189 NGFIDVSnrkgkFEYRVTEESLMdrltTNAHEACLSIRE-NCRVLTVHGSNDRIV---HVTEASEFAKQIKnhKLYVIEG 264
Cdd:COG1073   159 AYLPGVP-----YLPNVRLASLL----NDEFDPLAKIEKiSRPLLFIHGEKDEAVpfyMSEDLYEAAAEPK--ELLIVPG 227

                         250       260
                  ....*....|....*....|...
gi 1063731405 265 ADHE--FTSHQHQLASIVLSFFK 285
Cdd:COG1073   228 AGHVdlYDRPEEEYFDKLAEFFK 250
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 37-285 1.47e-26

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 105.00  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  37 IQHQRVVIENSHGEKLVGVLH----DTGSTETVVICHGFRSSKNRipMLTIASFFERAMISSFRFDFAGNGESQGSF-QY 111
Cdd:COG1073     8 VNKEDVTFKSRDGIKLAGDLYlpagASKKYPAVVVAHGNGGVKEQ--RALYAQRLAELGFNVLAFDYRGYGESEGEPrEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 112 GNYRRevEDLRSVLQHLR---GVNRVISAIIGHSKGGNVVLLYAAKYNDVQTVVNISGrfFLDRGiefRLGKDYFKRIKD 188
Cdd:COG1073    86 GSPER--RDARAAVDYLRtlpGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSP--FTSLE---DLAAQRAKEARG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 189 NGFIDVSnrkgkFEYRVTEESLMdrltTNAHEACLSIRE-NCRVLTVHGSNDRIV---HVTEASEFAKQIKnhKLYVIEG 264
Cdd:COG1073   159 AYLPGVP-----YLPNVRLASLL----NDEFDPLAKIEKiSRPLLFIHGEKDEAVpfyMSEDLYEAAAEPK--ELLIVPG 227

                         250       260
                  ....*....|....*....|...
gi 1063731405 265 ADHE--FTSHQHQLASIVLSFFK 285
Cdd:COG1073   228 AGHVdlYDRPEEEYFDKLAEFFK 250
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 64-268 8.93e-15

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: 72.25  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  64 TVVICHGFRSSKNRipMLTIASFFERAMISSFRFDFAGNGESQGSFQY-GNYRREVEDLRSVLQHLR----GVNRVIsai 138
Cdd:pfam12146   6 VVVLVHGLGEHSGR--YAHLADALAAQGFAVYAYDHRGHGRSDGKRGHvPSFDDYVDDLDTFVDKIReehpGLPLFL--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 139 IGHSKGGNVVLLYAAKY-NDVQTVV---------------------NISGRFFLDRGIEFRLGKDYfkRIKDNGFID--- 193
Cdd:pfam12146  81 LGHSMGGLIAALYALRYpDKVDGLIlsapalkikpylappilkllaKLLGKLFPRLRVPNNLLPDS--LSRDPEVVAaya 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 194 -VSNRKGKFEYRVTEESL--MDRLTTNAHEACLSIrencrvLTVHGSNDRIVHVTEASEFAKQI--KNHKLYVIEGADHE 268
Cdd:pfam12146 159 aDPLVHGGISARTLYELLdaGERLLRRAAAITVPL------LLLHGGADRVVDPAGSREFYERAgsTDKTLKLYPGLYHE 232
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 37-285 1.47e-26

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 105.00  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  37 IQHQRVVIENSHGEKLVGVLH----DTGSTETVVICHGFRSSKNRipMLTIASFFERAMISSFRFDFAGNGESQGSF-QY 111
Cdd:COG1073     8 VNKEDVTFKSRDGIKLAGDLYlpagASKKYPAVVVAHGNGGVKEQ--RALYAQRLAELGFNVLAFDYRGYGESEGEPrEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 112 GNYRRevEDLRSVLQHLR---GVNRVISAIIGHSKGGNVVLLYAAKYNDVQTVVNISGrfFLDRGiefRLGKDYFKRIKD 188
Cdd:COG1073    86 GSPER--RDARAAVDYLRtlpGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSP--FTSLE---DLAAQRAKEARG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 189 NGFIDVSnrkgkFEYRVTEESLMdrltTNAHEACLSIRE-NCRVLTVHGSNDRIV---HVTEASEFAKQIKnhKLYVIEG 264
Cdd:COG1073   159 AYLPGVP-----YLPNVRLASLL----NDEFDPLAKIEKiSRPLLFIHGEKDEAVpfyMSEDLYEAAAEPK--ELLIVPG 227

                         250       260
                  ....*....|....*....|...
gi 1063731405 265 ADHE--FTSHQHQLASIVLSFFK 285
Cdd:COG1073   228 AGHVdlYDRPEEEYFDKLAEFFK 250
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
44-285 3.81e-21

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 90.08  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  44 IENSHGEKLVGVLH---DTGSTETVVICHGFRSSKNRiPMLTIASFFERAMISSFRFDFAGNGESQGSFqygnYRREVED 120
Cdd:COG1506     2 FKSADGTTLPGWLYlpaDGKKYPVVVYVHGGPGSRDD-SFLPLAQALASRGYAVLAPDYRGYGESAGDW----GGDEVDD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 121 LRSVLQHLR-----GVNRVisAIIGHSKGGNVVLLYAAKYND-VQTVVNISGrfFLDRGIEFRLGKDYFKRIKDNgfidv 194
Cdd:COG1506    77 VLAAIDYLAarpyvDPDRI--GIYGHSYGGYMALLAAARHPDrFKAAVALAG--VSDLRSYYGTTREYTERLMGG----- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 195 snrkgkfeYRVTEESLMDR-LTTNAHeaclsiRENCRVLTVHGSNDRIVHVTEASEFAKQI----KNHKLYVIEGADHEF 269
Cdd:COG1506   148 --------PWEDPEAYAARsPLAYAD------KLKTPLLLIHGEADDRVPPEQAERLYEALkkagKPVELLVYPGEGHGF 213

                         250
                  ....*....|....*..
gi 1063731405 270 TSHQH-QLASIVLSFFK 285
Cdd:COG1506   214 SGAGApDYLERILDFLD 230
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
38-285 7.26e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 88.91  E-value: 7.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  38 QHQRVVIENSHGEKLVGVLH--DTGSTETVVICHGFRSSKNRipMLTIASFFERAMISSFRFDFAGNGESQGSFQY-GNY 114
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWrpAGSPRGTVVLVHGLGEHSGR--YAELAEALAAAGYAVLAFDLRGHGRSDGPRGHvDSF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 115 RREVEDLRSVLQHLRGVN--RVIsaIIGHSKGGNVVLLYAAKYND-VQTVVNISGRFFLDRGIEFRLGkdyfkrikdngf 191
Cdd:COG2267    80 DDYVDDLRAALDALRARPglPVV--LLGHSMGGLIALLYAARYPDrVAGLVLLAPAYRADPLLGPSAR------------ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 192 idvsnrkgkfeyrvteesLMDRLTTNAHEACLsireNCRVLTVHGSNDRIVHVTEASEFAKQI-KNHKLYVIEGADHEFT 270
Cdd:COG2267   146 ------------------WLRALRLAEALARI----DVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELL 203

                         250
                  ....*....|....*..
gi 1063731405 271 --SHQHQLASIVLSFFK 285
Cdd:COG2267   204 nePAREEVLAAILAWLE 220
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
41-285 1.02e-16

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 77.12  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  41 RVVIENSHGeKLVGVLH--DTGSTETVVICH------GFRssKNRIPMlTIASFFERAMISSFRFDFAGNGESQGSFQYG 112
Cdd:COG2945     1 KVLINGPAG-RLEGRLDlpEGPPRGVALILHphplfgGTM--DNKVVY-TLARALVAAGFAVLRFNFRGVGRSEGEFDEG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 113 nyRREVEDLRSVLQHLRGVNRVISAIIGHSKGGNVVLLYAAKYNDVQTVVNIS---GRFfldrgiefrlgkdyfkrikDN 189
Cdd:COG2945    77 --RGELDDAAAALDWLRAQNPLPLWLAGFSFGAYVALQLAMRLPEVEGLILVAppvNRY-------------------DF 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 190 GFIDvsnrkgkfeyrvteeslmdrlttnaheaclsiRENCRVLTVHGSNDRIVHVTEASE-FAKQIKNHKLYVIEGADHE 268
Cdd:COG2945   136 SFLA--------------------------------PCPAPTLVIHGEQDEVVPPAEVLDwARPLSPPLPVVVVPGADHF 183

                         250
                  ....*....|....*..
gi 1063731405 269 FTSHQHQLASIVLSFFK 285
Cdd:COG2945   184 FHGKLDELKELVARYLP 200
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 57-285 2.88e-16

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: 76.19  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  57 HDTGST-ETVVICHGFRSSknripmltiASFFER---AMISSFR---FDFAGNGESQGSFQYGNYRREVEDLRSVLQHLr 129
Cdd:COG0596    17 REAGPDgPPVVLLHGLPGS---------SYEWRPlipALAAGYRviaPDLRGHGRSDKPAGGYTLDDLADDLAALLDAL- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 130 GVNRVIsaIIGHSKGGNVVLLYAAKYND-VQTVVNISG--RFFLDRGIEFRLGKDYFKRikdngfidvsnrkgkfeyrvt 206
Cdd:COG0596    87 GLERVV--LVGHSMGGMVALELAARHPErVAGLVLVDEvlAALAEPLRRPGLAPEALAA--------------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 207 eesLMDRLTTNAHEACLSiRENCRVLTVHGSNDRIVHVTEASEFAKQIKNHKLYVIEGADHE-FTSHQHQLASIVLSFFK 285
Cdd:COG0596   144 ---LLRALARTDLRERLA-RITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFpPLEQPEAFAAALRDFLA 219
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 64-268 8.93e-15

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: 72.25  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  64 TVVICHGFRSSKNRipMLTIASFFERAMISSFRFDFAGNGESQGSFQY-GNYRREVEDLRSVLQHLR----GVNRVIsai 138
Cdd:pfam12146   6 VVVLVHGLGEHSGR--YAHLADALAAQGFAVYAYDHRGHGRSDGKRGHvPSFDDYVDDLDTFVDKIReehpGLPLFL--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 139 IGHSKGGNVVLLYAAKY-NDVQTVV---------------------NISGRFFLDRGIEFRLGKDYfkRIKDNGFID--- 193
Cdd:pfam12146  81 LGHSMGGLIAALYALRYpDKVDGLIlsapalkikpylappilkllaKLLGKLFPRLRVPNNLLPDS--LSRDPEVVAaya 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 194 -VSNRKGKFEYRVTEESL--MDRLTTNAHEACLSIrencrvLTVHGSNDRIVHVTEASEFAKQI--KNHKLYVIEGADHE 268
Cdd:pfam12146 159 aDPLVHGGISARTLYELLdaGERLLRRAAAITVPL------LLLHGGADRVVDPAGSREFYERAgsTDKTLKLYPGLYHE 232
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 64-269 4.56e-11

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: 61.75  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  64 TVVICHGFRSSKNrIPMlTIASFFERAMISSFRFDFAGNGESQGSFQYGNYRRE--VEDLRSVLQHLrGVNRVIsaIIGH 141
Cdd:pfam00561   2 PVLLLHGLPGSSD-LWR-KLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEAL-GLEKVN--LVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 142 SKGGNVVLLYAAKYND-VQTVVNISGR---FFLDRGIEFRLGK--DYFKRIKDNGFIDVSNRKGKFEYR--VTEESLMDR 213
Cdd:pfam00561  77 SMGGLIALAYAAKYPDrVKALVLLGALdppHELDEADRFILALfpGFFDGFVADFAPNPLGRLVAKLLAllLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 214 L------------------TTNAHEACLSIRENCR----------VLTVHGSNDRIVHVTEASEFAKQIKNHKLYVIEGA 265
Cdd:pfam00561 157 LpllnkrfpsgdyalakslVTGALLFIETWSTELRakflgrldepTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDA 236


                  ....
gi 1063731405 266 DHEF 269
Cdd:pfam00561 237 GHFA 240
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
37-270 1.09e-10

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 60.37  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  37 IQHQRVVIENSHGEKLVGVLH---DTGSTETVVICHGFRSSKNRIpmLTIASFFERA-----MISSFRFDFAGNGESQGS 108
Cdd:COG0412     1 MTTETVTIPTPDGVTLPGYLArpaGGGPRPGVVVLHEIFGLNPHI--RDVARRLAAAgyvvlAPDLYGRGGPGDDPDEAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 109 FQYGNYRRE--VEDLRSVLQHLRGVNRVIS---AIIGHSKGGNVVLLYAAKYNDVQTVVNISGRFFLDRGIefrlgkDYF 183
Cdd:COG0412    79 ALMGALDPEllAADLRAALDWLKAQPEVDAgrvGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADDLL------DLA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 184 KRIKdngfidvsnrkgkfeyrvteeslmdrlttnaheaclsirenCRVLTVHGSNDRIVHVTEASEFAKQIK----NHKL 259
Cdd:COG0412   153 ARIK-----------------------------------------APVLLLYGEKDPLVPPEQVAALEAALAaagvDVEL 191

                         250
                  ....*....|.
gi 1063731405 260 YVIEGADHEFT 270
Cdd:COG0412   192 HVYPGAGHGFT 202
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 65-166 1.16e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.58  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  65 VVICHGFRSSKNRipMLTIASFFERAMISSFRFDFagngesqGSFQYGNYRReVEDLRSVLQHLR---GVNRVIsaIIGH 141
Cdd:COG1075     8 VVLVHGLGGSAAS--WAPLAPRLRAAGYPVYALNY-------PSTNGSIEDS-AEQLAAFVDAVLaatGAEKVD--LVGH 75

                          90       100
                  ....*....|....*....|....*...
gi 1063731405 142 SKGGNVVLLYAAKY---NDVQTVVNISG 166
Cdd:COG1075    76 SMGGLVARYYLKRLggaAKVARVVTLGT 103
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
106-285 2.11e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 41.83  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 106 QGSFQYGNYrrEVEDLRSVLQHL--RGV---NRVisAIIGHSKGGNVVLLYAAKYNDVQTVVnISGRFFLDRgiefrLGK 180
Cdd:pfam00326  35 AGKGDLGQN--EFDDFIAAAEYLieQGYtdpDRL--AIWGGSYGGYLTGAALNQRPDLFKAA-VAHVPVVDW-----LAY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 181 DYFKRIK-DNGFIDVSNRKGKFEYRVTEESLmdrltTNAHEaclsIRENCRVLTVHGSNDRIVHVTEASEFAKQI----K 255
Cdd:pfam00326 105 MSDTSLPfTERYMEWGNPWDNEEGYDYLSPY-----SPADN----VKVYPPLLLIHGLLDDRVPPWQSLKLVAALqrkgV 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063731405 256 NHKLYVIEGADHEFTSHQHQLASI--VLSFFK 285
Cdd:pfam00326 176 PFLLLIFPDEGHGIGKPRNKVEEYarELAFLL 207
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
34-165 2.79e-04

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 42.05  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405  34 KSEIQHQRVVIENSHGE--KLVGVLHDTGSTETVVICHGFRSSKNRIPMLTIASFFERAMISSFRFDFAGNGE----SQG 107
Cdd:COG0429    31 RPALPYRRERLELPDGDfvDLDWSDPPAPSKPLVVLLHGLEGSSDSHYARGLARALYARGWDVVRLNFRGCGGepnlLPR 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063731405 108 SFQYGnyrrEVEDLRSVLQHL--RGVNRVIsAIIGHSKGGNVVLLYAAKY----NDVQTVVNIS 165
Cdd:COG0429   111 LYHSG----DTEDLVWVLAHLraRYPYAPL-YAVGFSLGGNLLLKYLGEQgddaPPLKAAVAVS 169
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
 137-267 1.57e-03

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: 39.19  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731405 137 AIIGHSKGGNVVLLYAAKYNDVQTVVNISGRFFLDRGIEFRlgKD-YFKRIKDNGFIDVSNRKGKFEYRVTEESLMDRLT 215
Cdd:pfam08840  25 GLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVY--KDnPLPPLGEGMRRIKVNKDGLLDIRDMFNDPLSKPD 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063731405 216 tnaHEACLSI-RENCRVLTVHGSNDrivHVTEASEFAKQI--------KNHKLYVI--EGADH 267
Cdd:pfam08840 103 ---PKSLIPVeRAKGPFLFVVGQDD---HNWPSVFYAKKAcerlqkhgKEVEVQLVcyPGAGH 159
 
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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