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Conserved domains on  [gi|79313171|ref|NP_001030665|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
190-476 1.42e-15

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 76.39  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   190 LIVPHSFLSSRLAGIpGVKESLLKDyGVRLVSYDLPGFGESDPHRARN---LSSSASDMIDLAAALGIvDKFWLLGYSSG 266
Cdd:pfam00561   3 VLLLHGLPGSSDLWR-KLAPALARD-GFRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGL-EKVNLVGHSMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   267 SVHAWAAMRYFPDQIAGVAMVAPMINPYEPSMTKEEMAKTWEQWQRKrkfmyflarrwpsllpfsYRRSFLSGNLEPLdk 346
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDG------------------FVADFAPNPLGRL-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   347 wmsvslgekdklvTADPVFEDLYQRNVEESVRQGTAKPFVEEAALQVSNWGFSLpefhmqkkcrtNGVLSWLmsmYSESE 426
Cdd:pfam00561 140 -------------VAKLLALLLLRLRLLKALPLLNKRFPSGDYALAKSLVTGAL-----------LFIETWS---TELRA 192
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 79313171   427 CELIGFRKPIHIWQGMDDRVTPPSVTDYISRVIPEATVHRLPNEGHFSYF 476
Cdd:pfam00561 193 KFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
190-476 1.42e-15

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: 76.39  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   190 LIVPHSFLSSRLAGIpGVKESLLKDyGVRLVSYDLPGFGESDPHRARN---LSSSASDMIDLAAALGIvDKFWLLGYSSG 266
Cdd:pfam00561   3 VLLLHGLPGSSDLWR-KLAPALARD-GFRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGL-EKVNLVGHSMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   267 SVHAWAAMRYFPDQIAGVAMVAPMINPYEPSMTKEEMAKTWEQWQRKrkfmyflarrwpsllpfsYRRSFLSGNLEPLdk 346
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDG------------------FVADFAPNPLGRL-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   347 wmsvslgekdklvTADPVFEDLYQRNVEESVRQGTAKPFVEEAALQVSNWGFSLpefhmqkkcrtNGVLSWLmsmYSESE 426
Cdd:pfam00561 140 -------------VAKLLALLLLRLRLLKALPLLNKRFPSGDYALAKSLVTGAL-----------LFIETWS---TELRA 192
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 79313171   427 CELIGFRKPIHIWQGMDDRVTPPSVTDYISRVIPEATVHRLPNEGHFSYF 476
Cdd:pfam00561 193 KFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
170-304 9.55e-14

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: 70.42  E-value: 9.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171 170 DGRYLAYQELGVSADRarhsLIVPHSFLSSRLAGIPgVKESLLKDYgvRLVSYDLPGFGESD-PHRARNLSSSASDMIDL 248
Cdd:COG0596  10 DGVRLHYREAGPDGPP----VVLLHGLPGSSYEWRP-LIPALAAGY--RVIAPDLRGHGRSDkPAGGYTLDDLADDLAAL 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 79313171 249 AAALGIvDKFWLLGYSSGSVHAWAAMRYFPDQIAGVAMVAPMINPYEPSMTKEEMA 304
Cdd:COG0596  83 LDALGL-ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLA 137
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
170-289 5.39e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.24  E-value: 5.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171  170 DGRYLAYQELGVSADRArhsLIVPHSF---LSSRLAGIPGVKEsllkdyGVRLVSYDLPGFGESDPHRAR-NLSSSASDM 245
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTP---VVLIHGFggdLNNWLFNHAALAA------GRPVIALDLPGHGASSKAVGAgSLDELAAAV 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 79313171  246 IDLAAALGIvDKFWLLGYSSGSVHAWAAMRYFPDQIAGVAMVAP 289
Cdd:PRK14875 188 LAFLDALGI-ERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
190-476 1.42e-15

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: 76.39  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   190 LIVPHSFLSSRLAGIpGVKESLLKDyGVRLVSYDLPGFGESDPHRARN---LSSSASDMIDLAAALGIvDKFWLLGYSSG 266
Cdd:pfam00561   3 VLLLHGLPGSSDLWR-KLAPALARD-GFRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGL-EKVNLVGHSMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   267 SVHAWAAMRYFPDQIAGVAMVAPMINPYEPSMTKEEMAKTWEQWQRKrkfmyflarrwpsllpfsYRRSFLSGNLEPLdk 346
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDG------------------FVADFAPNPLGRL-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   347 wmsvslgekdklvTADPVFEDLYQRNVEESVRQGTAKPFVEEAALQVSNWGFSLpefhmqkkcrtNGVLSWLmsmYSESE 426
Cdd:pfam00561 140 -------------VAKLLALLLLRLRLLKALPLLNKRFPSGDYALAKSLVTGAL-----------LFIETWS---TELRA 192
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 79313171   427 CELIGFRKPIHIWQGMDDRVTPPSVTDYISRVIPEATVHRLPNEGHFSYF 476
Cdd:pfam00561 193 KFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
170-304 9.55e-14

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: 70.42  E-value: 9.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171 170 DGRYLAYQELGVSADRarhsLIVPHSFLSSRLAGIPgVKESLLKDYgvRLVSYDLPGFGESD-PHRARNLSSSASDMIDL 248
Cdd:COG0596  10 DGVRLHYREAGPDGPP----VVLLHGLPGSSYEWRP-LIPALAAGY--RVIAPDLRGHGRSDkPAGGYTLDDLADDLAAL 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 79313171 249 AAALGIvDKFWLLGYSSGSVHAWAAMRYFPDQIAGVAMVAPMINPYEPSMTKEEMA 304
Cdd:COG0596  83 LDALGL-ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLA 137
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
214-360 1.29e-08

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: 55.68  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   214 DYGVrlVSYDLPGFGESDPHRARnlSSSASDMI-DLAAALGIV------DKFWLLGYSSGSVHAWAAMRYFPDQIAGVAM 286
Cdd:pfam12146  31 GFAV--YAYDHRGHGRSDGKRGH--VPSFDDYVdDLDTFVDKIreehpgLPLFLLGHSMGGLIAALYALRYPDKVDGLIL 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79313171   287 VAPMINPYEPSMTKEemaktweqwqrKRKFMYFLARRWPSL-LPFSYRRSFLSGNLEPLDKWmsvslgEKDKLVT 360
Cdd:pfam12146 107 SAPALKIKPYLAPPI-----------LKLLAKLLGKLFPRLrVPNNLLPDSLSRDPEVVAAY------AADPLVH 164
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
216-289 2.63e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.54  E-value: 2.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171 216 GVRLVSYDLPGFGESDphRARNLSSSASDMI-DLAAALGIV-----DKFWLLGYSSGSVHAWAAMRYFPDQIAGVAMVAP 289
Cdd:COG2267  55 GYAVLAFDLRGHGRSD--GPRGHVDSFDDYVdDLRAALDALrarpgLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
212-293 6.04e-07

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 50.16  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171   212 LKDYGVRLVSYDLPGFGESDPHRARnlSSSASDMIDLAAALGIVDKFWLLGYSSGSVHAWAAMRYFPdqIAGVAMVAPMI 291
Cdd:pfam12697  17 LLAAGVAVLAPDLPGHGSSSPPPLD--LADLADLAALLDELGAARPVVLVGHSLGGAVALAAAAAAL--VVGVLVAPLAA 92

                  ..
gi 79313171   292 NP 293
Cdd:pfam12697  93 PP 94
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
170-289 5.39e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.24  E-value: 5.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171  170 DGRYLAYQELGVSADRArhsLIVPHSF---LSSRLAGIPGVKEsllkdyGVRLVSYDLPGFGESDPHRAR-NLSSSASDM 245
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTP---VVLIHGFggdLNNWLFNHAALAA------GRPVIALDLPGHGASSKAVGAgSLDELAAAV 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 79313171  246 IDLAAALGIvDKFWLLGYSSGSVHAWAAMRYFPDQIAGVAMVAP 289
Cdd:PRK14875 188 LAFLDALGI-ERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
215-318 1.32e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 40.39  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313171 215 YGVrlVSYDLPGFGESDPHRARNLSSSASDMIDLAAALGIVD--KFWLLGYSSGSVHAWAAMRYFPDQIAGVAMVAPMIN 292
Cdd:COG1506  52 YAV--LAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYVDpdRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSD 129
                        90       100
                ....*....|....*....|....*.
gi 79313171 293 PYEPSMTKEEMAKTWEQWQRKRKFMY 318
Cdd:COG1506 130 LRSYYGTTREYTERLMGGPWEDPEAY 155
YpfH COG0400
Predicted esterase [General function prediction only];
222-295 2.62e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.12  E-value: 2.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79313171 222 YDLPGF-GESDPHRARNLSSSASDMID-LAAALGI-VDKFWLLGYSSGSVHAWAAMRYFPDQIAGVAMVAPMINPYE 295
Cdd:COG0400  52 FDLSFLeGREDEEGLAAAAEALAAFIDeLEARYGIdPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEE 128
 
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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