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Conserved domains on  [gi|767915328|ref|XP_011531438|]
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protein ABHD1 isoform X2 [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];
58-248 4.25e-45

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: 155.30  E-value: 4.25e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  58 ITTETFYPTLWCFEGRLQSIFQVLLQSQPLVLYQSDILQTPDGGQLLLDWAkqpdssqDPDPTTQPIVLLLPGITGSSQE 137
Cdd:COG0429    4 LSTSPFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWS-------DPPAPSKPLVVLLHGLEGSSDS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 138 TYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLA-QA 216
Cdd:COG0429   77 HYARGLARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGeQG 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767915328 217 RQAAGLVAALTLSACWDSFETTRSLETPLNSL 248
Cdd:COG0429  157 DDAPPLKAAVAVSPPLDLAASADRLERGFNRL 188
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
58-248 4.25e-45

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 155.30  E-value: 4.25e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  58 ITTETFYPTLWCFEGRLQSIFQVLLQSQPLVLYQSDILQTPDGGQLLLDWAkqpdssqDPDPTTQPIVLLLPGITGSSQE 137
Cdd:COG0429    4 LSTSPFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWS-------DPPAPSKPLVVLLHGLEGSSDS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 138 TYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLA-QA 216
Cdd:COG0429   77 HYARGLARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGeQG 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767915328 217 RQAAGLVAALTLSACWDSFETTRSLETPLNSL 248
Cdd:COG0429  157 DDAPPLKAAVAVSPPLDLAASADRLERGFNRL 188
PLN02511 PLN02511
hydrolase
 50-228 7.44e-41

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 146.08  E-value: 7.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  50 AFLEPHCSITTETFYPTLWCFEGRLQSIFQVLLQSQPLVLYQSDILQTPDGGQLLLDWakqPDSSQDPDPTTQPIVLLLP 129
Cdd:PLN02511  31 DSFLPKFKSLERPYDAFPLLGNRHVETIFASFFRSLPAVRYRRECLRTPDGGAVALDW---VSGDDRALPADAPVLILLP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 130 GITGSSQETYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILV 209
Cdd:PLN02511 108 GLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGCADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGWSLGANIL 187

                        170
                 ....*....|....*....
gi 767915328 210 LNHLAQARQAAGLVAALTL 228
Cdd:PLN02511 188 VNYLGEEGENCPLSGAVSL 206
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 123-249 1.69e-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: 51.35  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  123 PIVLLLPGITGSSQETYvlHLVNQALRDGYQAVVFNNRGC-RGEELRTHRAFCasnTEDLETVVNHIKHRYPQAPLLAVG 201
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFgKSSRPKAQDDYR---TDDLAEDLEYILEALGLEKVNLVG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767915328  202 ISFGGILVLNHLAQARQaagLVAALTL-SACWDSFETTRSLETPLNSLL 249
Cdd:pfam00561  76 HSMGGLIALAYAAKYPD---RVKALVLlGALDPPHELDEADRFILALFP 121
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
58-248 4.25e-45

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 155.30  E-value: 4.25e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  58 ITTETFYPTLWCFEGRLQSIFQVLLQSQPLVLYQSDILQTPDGGQLLLDWAkqpdssqDPDPTTQPIVLLLPGITGSSQE 137
Cdd:COG0429    4 LSTSPFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWS-------DPPAPSKPLVVLLHGLEGSSDS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 138 TYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLA-QA 216
Cdd:COG0429   77 HYARGLARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGeQG 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767915328 217 RQAAGLVAALTLSACWDSFETTRSLETPLNSL 248
Cdd:COG0429  157 DDAPPLKAAVAVSPPLDLAASADRLERGFNRL 188
PLN02511 PLN02511
hydrolase
 50-228 7.44e-41

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 146.08  E-value: 7.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  50 AFLEPHCSITTETFYPTLWCFEGRLQSIFQVLLQSQPLVLYQSDILQTPDGGQLLLDWakqPDSSQDPDPTTQPIVLLLP 129
Cdd:PLN02511  31 DSFLPKFKSLERPYDAFPLLGNRHVETIFASFFRSLPAVRYRRECLRTPDGGAVALDW---VSGDDRALPADAPVLILLP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 130 GITGSSQETYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILV 209
Cdd:PLN02511 108 GLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGCADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGWSLGANIL 187

                        170
                 ....*....|....*....
gi 767915328 210 LNHLAQARQAAGLVAALTL 228
Cdd:PLN02511 188 VNYLGEEGENCPLSGAVSL 206
PRK10985 PRK10985
putative hydrolase; Provisional
 61-230 4.43e-21

putative hydrolase; Provisional


Pssm-ID: 182883  Cd Length: 324  Bit Score: 91.17  E-value: 4.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  61 ETFYPTLWCFEGRLQSIFQVLLQSQPLVLYQSDILQTPDGGQLLLDWAKQPDSSQDpdpttQPIVLLLPGITGSSQETYV 140
Cdd:PRK10985   2 AEFTPMRGASNPHLQTLLPRLIRRKVLFTPYWQRLELPDGDFVDLAWSEDPAQARH-----KPRLVLFHGLEGSFNSPYA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 141 LHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLAQARQAA 220
Cdd:PRK10985  77 HGLLEAAQKRGWLGVVMHFRGCSGEPNRLHRIYHSGETEDARFFLRWLQREFGHVPTAAVGYSLGGNMLACLLAKEGDDL 156

                        170
                 ....*....|
gi 767915328 221 GLVAALTLSA 230
Cdd:PRK10985 157 PLDAAVIVSA 166
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
95-230 4.06e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 61.56  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  95 LQTPDGGQL-LLDWAkqpdssqdPDPTTQPIVLLLPGITGSSqETYvLHLVNQALRDGYQAVVFNNRGC-RGEELRTHRA 172
Cdd:COG2267    8 LPTRDGLRLrGRRWR--------PAGSPRGTVVLVHGLGEHS-GRY-AELAEALAAAGYAVLAFDLRGHgRSDGPRGHVD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767915328 173 FCASNTEDLETVVNHIKHRyPQAPLLAVGISFGGILVLNHLAQARQAaglVAALTLSA 230
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.
 123-249 1.69e-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: 51.35  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  123 PIVLLLPGITGSSQETYvlHLVNQALRDGYQAVVFNNRGC-RGEELRTHRAFCasnTEDLETVVNHIKHRYPQAPLLAVG 201
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFgKSSRPKAQDDYR---TDDLAEDLEYILEALGLEKVNLVG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767915328  202 ISFGGILVLNHLAQARQaagLVAALTL-SACWDSFETTRSLETPLNSLL 249
Cdd:pfam00561  76 HSMGGLIALAYAAKYPD---RVKALVLlGALDPPHELDEADRFILALFP 121
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 123-228 5.03e-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: 46.53  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 123 PIVLLLPGITGSSqetYVLHLVNQALRDGYQAVVFNNRGC----RGEELRTHRAFCAsnteDLETVVNHIKHRypqaPLL 198
Cdd:COG0596   24 PPVVLLHGLPGSS---YEWRPLIPALAAGYRVIAPDLRGHgrsdKPAGGYTLDDLAD----DLAALLDALGLE----RVV 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 767915328 199 AVGISFGGILVLNHlaqARQAAGLVAALTL 228
Cdd:COG0596   93 LVGHSMGGMVALEL---AARHPERVAGLVL 119
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 125-232 1.25e-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: 45.54  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  125 VLLLPGITgssqetYVLHLVNQALRDGYQAVVFNNRGCrGEELRTHRAFcasntEDLETVVNHIKHRYPQAPLLAVGISF 204
Cdd:pfam12697   1 VVLVHGAG------LSAAPLAALLAAGVAVLAPDLPGH-GSSSPPPLDL-----ADLADLAALLDELGAARPVVLVGHSL 68

                          90       100
                  ....*....|....*....|....*...
gi 767915328  205 GGILVLNHLAQARQAAGLVAALTLSACW 232
Cdd:pfam12697  69 GGAVALAAAAAALVVGVLVAPLAAPPGL 96
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
117-233 2.32e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 44.62  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 117 PDPTTQPIVLLLPGITGSSQETYvLHLVNQALRDGYQAVVFNNRGcRGEELRTHRafcASNTEDLETVVNHIKHR--YPQ 194
Cdd:COG1506   18 ADGKKYPVVVYVHGGPGSRDDSF-LPLAQALASRGYAVLAPDYRG-YGESAGDWG---GDEVDDVLAAIDYLAARpyVDP 92

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767915328 195 APLLAVGISFGGILVLnhLAQARQAAGLVAALTLSACWD 233
Cdd:COG1506   93 DRIGIYGHSYGGYMAL--LAAARHPDRFKAAVALAGVSD 129
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 124-230 5.27e-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: 43.74  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  124 IVLLLPGITGSSQeTYvLHLVNQALRDGYQAVVFNNRGCRGEElrTHRAFCAS---NTEDLETVVNHIKHRYPQAPLLAV 200
Cdd:pfam12146   6 VVVLVHGLGEHSG-RY-AHLADALAAQGFAVYAYDHRGHGRSD--GKRGHVPSfddYVDDLDTFVDKIREEHPGLPLFLL 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 767915328  201 GISFGGILVLNHLAQARQAaglVAALTLSA 230
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDK---VDGLILSA 108
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
95-224 7.77e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.03  E-value: 7.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328  95 LQTPDGGQLLLDWAKqpdssqDPDPTTQPIVLLLPGITGSSQetYVLHLVNQALRDGYQAVVFN-----NRGCRGEELRT 169
Cdd:COG0412    8 IPTPDGVTLPGYLAR------PAGGGPRPGVVVLHEIFGLNP--HIRDVARRLAAAGYVVLAPDlygrgGPGDDPDEARA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915328 170 H--RAFCASNTEDLETVVNHIKHR--YPQAPLLAVGISFGGILVLNHLAQARQAAGLVA 224
Cdd:COG0412   80 LmgALDPELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVS 138
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 117-227 8.73e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 38.27  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 117 PDPTTQPIVLLlPGITGSSQETYVlhLVNQALRDGYQAVVFNnrgcrgeeLRTHRAFCASNTEDLETVVNHIKHRYPQAP 196
Cdd:COG1075    1 YAATRYPVVLV-HGLGGSAASWAP--LAPRLRAAGYPVYALN--------YPSTNGSIEDSAEQLAAFVDAVLAATGAEK 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915328 197 LLAVGISFGGiLVLNHLAQARQAAGLVAALT 227
Cdd:COG1075   70 VDLVGHSMGG-LVARYYLKRLGGAAKVARVV 99
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
121-233 2.23e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.77  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915328 121 TQPIVLLLPGITGSSQEtyVLHLVNQALRDGYQAVVFNNRG--CRGEELRTHRAfcASNTEDLETVVNHIKHRYPQapLL 198
Cdd:COG1647   14 GRKGVLLLHGFTGSPAE--MRPLAEALAKAGYTVYAPRLPGhgTSPEDLLKTTW--EDWLEDVEEAYEILKAGYDK--VI 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767915328 199 AVGISFGGILVLNHLAQARQAAGLVaalTLSACWD 233
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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