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Conserved domains on  [gi|767915332|ref|XP_011531440|]
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protein ABHD1 isoform X4 [Homo sapiens]

Protein Classification

alpha/beta fold hydrolase family protein( domain architecture ID 1903474)

alpha/beta fold hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad; similar to monoacylglycerol lipase ABHD2

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016787
PubMed:  1409539|12369917|10607665
SCOP:  3000102

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YheT super family cl43141
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
5-185 1.54e-38

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


The actual alignment was detected with superfamily member COG0429:

Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 136.43  E-value: 1.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332   5 QT--PSLCSWLLPLPSTWattghvcfsDILQTPDGGQLLLDWAkqpdssqDPDPTTQPIVLLLPGITGSSQETYVLHLVN 82
Cdd:COG0429   21 QTiyPSLFRRRPALPYRR---------ERLELPDGDFVDLDWS-------DPPAPSKPLVVLLHGLEGSSDSHYARGLAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  83 QALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLA-QARQAAGLVA 161
Cdd:COG0429   85 ALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGeQGDDAPPLKA 164

                        170       180
                 ....*....|....*....|....
gi 767915332 162 ALTLSACWDSFETTRSLETPLNSL 185
Cdd:COG0429  165 AVAVSPPLDLAASADRLERGFNRL 188
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
5-185 1.54e-38

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 136.43  E-value: 1.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332   5 QT--PSLCSWLLPLPSTWattghvcfsDILQTPDGGQLLLDWAkqpdssqDPDPTTQPIVLLLPGITGSSQETYVLHLVN 82
Cdd:COG0429   21 QTiyPSLFRRRPALPYRR---------ERLELPDGDFVDLDWS-------DPPAPSKPLVVLLHGLEGSSDSHYARGLAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  83 QALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLA-QARQAAGLVA 161
Cdd:COG0429   85 ALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGeQGDDAPPLKA 164

                        170       180
                 ....*....|....*....|....
gi 767915332 162 ALTLSACWDSFETTRSLETPLNSL 185
Cdd:COG0429  165 AVAVSPPLDLAASADRLERGFNRL 188
PLN02511 PLN02511
hydrolase
 30-165 1.71e-36

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 132.60  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  30 DILQTPDGGQLLLDWakqPDSSQDPDPTTQPIVLLLPGITGSSQETYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRA 109
Cdd:PLN02511  74 ECLRTPDGGAVALDW---VSGDDRALPADAPVLILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGCADSPVTTPQF 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767915332 110 FCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLAQARQAAGLVAALTL 165
Cdd:PLN02511 151 YSASFTGDLRQVVDHVAGRYPSANLYAAGWSLGANILVNYLGEEGENCPLSGAVSL 206
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 60-205 3.65e-08

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: 52.51  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332   60 PIVLLLPGITGSSQETYvlHLVNQALRDGYQAVVFNNRGC-RGEELRTHRAFCasnTEDLETVVNHIKHRYPQAPLLAVG 138
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFgKSSRPKAQDDYR---TDDLAEDLEYILEALGLEKVNLVG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915332  139 ISFGGILVLNHLAQARQaagLVAALTL-SACWDSFETTRSLETPLNSLLFNQPLTAGLCQLVERNRKV 205
Cdd:pfam00561  76 HSMGGLIALAYAAKYPD---RVKALVLlGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLV 140
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
5-185 1.54e-38

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 136.43  E-value: 1.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332   5 QT--PSLCSWLLPLPSTWattghvcfsDILQTPDGGQLLLDWAkqpdssqDPDPTTQPIVLLLPGITGSSQETYVLHLVN 82
Cdd:COG0429   21 QTiyPSLFRRRPALPYRR---------ERLELPDGDFVDLDWS-------DPPAPSKPLVVLLHGLEGSSDSHYARGLAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  83 QALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLA-QARQAAGLVA 161
Cdd:COG0429   85 ALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGeQGDDAPPLKA 164

                        170       180
                 ....*....|....*....|....
gi 767915332 162 ALTLSACWDSFETTRSLETPLNSL 185
Cdd:COG0429  165 AVAVSPPLDLAASADRLERGFNRL 188
PLN02511 PLN02511
hydrolase
 30-165 1.71e-36

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 132.60  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  30 DILQTPDGGQLLLDWakqPDSSQDPDPTTQPIVLLLPGITGSSQETYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRA 109
Cdd:PLN02511  74 ECLRTPDGGAVALDW---VSGDDRALPADAPVLILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGCADSPVTTPQF 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767915332 110 FCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLAQARQAAGLVAALTL 165
Cdd:PLN02511 151 YSASFTGDLRQVVDHVAGRYPSANLYAAGWSLGANILVNYLGEEGENCPLSGAVSL 206
PRK10985 PRK10985
putative hydrolase; Provisional
 32-167 7.76e-21

putative hydrolase; Provisional


Pssm-ID: 182883  Cd Length: 324  Bit Score: 89.25  E-value: 7.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  32 LQTPDGGQLLLDWAKQPDSSQDpdpttQPIVLLLPGITGSSQETYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFC 111
Cdd:PRK10985  36 LELPDGDFVDLAWSEDPAQARH-----KPRLVLFHGLEGSFNSPYAHGLLEAAQKRGWLGVVMHFRGCSGEPNRLHRIYH 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767915332 112 ASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLAQARQAAGLVAALTLSA 167
Cdd:PRK10985 111 SGETEDARFFLRWLQREFGHVPTAAVGYSLGGNMLACLLAKEGDDLPLDAAVIVSA 166
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
32-167 3.42e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 61.17  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  32 LQTPDGGQL-LLDWAkqpdssqdPDPTTQPIVLLLPGITGSSqETYvLHLVNQALRDGYQAVVFNNRGC-RGEELRTHRA 109
Cdd:COG2267    8 LPTRDGLRLrGRRWR--------PAGSPRGTVVLVHGLGEHS-GRY-AELAEALAAAGYAVLAFDLRGHgRSDGPRGHVD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767915332 110 FCASNTEDLETVVNHIKHRyPQAPLLAVGISFGGILVLNHLAQARQAaglVAALTLSA 167
Cdd:COG2267   78 SFDDYVDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDR---VAGLVLLA 131
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 60-205 3.65e-08

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: 52.51  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332   60 PIVLLLPGITGSSQETYvlHLVNQALRDGYQAVVFNNRGC-RGEELRTHRAFCasnTEDLETVVNHIKHRYPQAPLLAVG 138
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFgKSSRPKAQDDYR---TDDLAEDLEYILEALGLEKVNLVG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915332  139 ISFGGILVLNHLAQARQaagLVAALTL-SACWDSFETTRSLETPLNSLLFNQPLTAGLCQLVERNRKV 205
Cdd:pfam00561  76 HSMGGLIALAYAAKYPD---RVKALVLlGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLV 140
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 60-165 6.62e-06

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: 45.76  E-value: 6.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  60 PIVLLLPGITGSSqetYVLHLVNQALRDGYQAVVFNNRGC----RGEELRTHRAFCAsnteDLETVVNHIKHRypqaPLL 135
Cdd:COG0596   24 PPVVLLHGLPGSS---YEWRPLIPALAAGYRVIAPDLRGHgrsdKPAGGYTLDDLAD----DLAALLDALGLE----RVV 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 767915332 136 AVGISFGGILVLNHlaqARQAAGLVAALTL 165
Cdd:COG0596   93 LVGHSMGGMVALEL---AARHPERVAGLVL 119
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 61-208 1.18e-05

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: 45.28  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332   61 IVLLLPGITGSSQeTYvLHLVNQALRDGYQAVVFNNRGCRGEElrTHRAFCAS---NTEDLETVVNHIKHRYPQAPLLAV 137
Cdd:pfam12146   6 VVVLVHGLGEHSG-RY-AHLADALAAQGFAVYAYDHRGHGRSD--GKRGHVPSfddYVDDLDTFVDKIREEHPGLPLFLL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915332  138 GISFGGILVLNHLAQ-ARQAAGLVaaLTLSACWDSFETTRS---LETPLNSLLF--NQPLTAGLCQLVERNRKVIEK 208
Cdd:pfam12146  82 GHSMGGLIAALYALRyPDKVDGLI--LSAPALKIKPYLAPPilkLLAKLLGKLFprLRVPNNLLPDSLSRDPEVVAA 156
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 62-169 1.50e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 44.77  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332   62 VLLLPGITgssqetYVLHLVNQALRDGYQAVVFNNRGCrGEELRTHRAFcasntEDLETVVNHIKHRYPQAPLLAVGISF 141
Cdd:pfam12697   1 VVLVHGAG------LSAAPLAALLAAGVAVLAPDLPGH-GSSSPPPLDL-----ADLADLAALLDELGAARPVVLVGHSL 68

                          90       100
                  ....*....|....*....|....*...
gi 767915332  142 GGILVLNHLAQARQAAGLVAALTLSACW 169
Cdd:pfam12697  69 GGAVALAAAAAALVVGVLVAPLAAPPGL 96
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
54-170 1.62e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 44.62  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  54 PDPTTQPIVLLLPGITGSSQETYvLHLVNQALRDGYQAVVFNNRGcRGEELRTHRafcASNTEDLETVVNHIKHR--YPQ 131
Cdd:COG1506   18 ADGKKYPVVVYVHGGPGSRDDSF-LPLAQALASRGYAVLAPDYRG-YGESAGDWG---GDEVDDVLAAIDYLAARpyVDP 92

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767915332 132 APLLAVGISFGGILVLnhLAQARQAAGLVAALTLSACWD 170
Cdd:COG1506   93 DRIGIYGHSYGGYMAL--LAAARHPDRFKAAVALAGVSD 129
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
32-161 6.00e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.03  E-value: 6.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  32 LQTPDGGQLLLDWAKqpdssqDPDPTTQPIVLLLPGITGSSQetYVLHLVNQALRDGYQAVVFN-----NRGCRGEELRT 106
Cdd:COG0412    8 IPTPDGVTLPGYLAR------PAGGGPRPGVVVLHEIFGLNP--HIRDVARRLAAAGYVVLAPDlygrgGPGDDPDEARA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915332 107 H--RAFCASNTEDLETVVNHIKHR--YPQAPLLAVGISFGGILVLNHLAQARQAAGLVA 161
Cdd:COG0412   80 LmgALDPELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVS 138
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 54-164 9.43e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.89  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  54 PDPTTQPIVLLlPGITGSSQETYVlhLVNQALRDGYQAVVFNnrgcrgeeLRTHRAFCASNTEDLETVVNHIKHRYPQAP 133
Cdd:COG1075    1 YAATRYPVVLV-HGLGGSAASWAP--LAPRLRAAGYPVYALN--------YPSTNGSIEDSAEQLAAFVDAVLAATGAEK 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915332 134 LLAVGISFGGiLVLNHLAQARQAAGLVAALT 164
Cdd:COG1075   70 VDLVGHSMGG-LVARYYLKRLGGAAKVARVV 99
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
58-170 1.67e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.77  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915332  58 TQPIVLLLPGITGSSQEtyVLHLVNQALRDGYQAVVFNNRG--CRGEELRTHRAfcASNTEDLETVVNHIKHRYPQapLL 135
Cdd:COG1647   14 GRKGVLLLHGFTGSPAE--MRPLAEALAKAGYTVYAPRLPGhgTSPEDLLKTTW--EDWLEDVEEAYEILKAGYDK--VI 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767915332 136 AVGISFGGILVLNHLAQARQAAGLVaalTLSACWD 170
Cdd:COG1647   88 VIGLSMGGLLALLLAARYPDVAGLV---LLSPALK 119
 
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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