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Conserved domains on  [gi|491853662|ref|WP_005634514|]
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MULTISPECIES: alpha/beta hydrolase [Parabacteroides]

Protein Classification

alpha/beta hydrolase( domain architecture ID 1001400)

alpha/beta hydrolase family protein catalyzes 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
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
240-281 2.47e-05

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


:

Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.39  E-value: 2.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491853662 240 VDYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDS-RFKVVIS 281
Cdd:COG1506   81 IDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPdRFKAAVA 123
DLH super family cl43135
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
240-334 6.12e-05

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


The actual alignment was detected with superfamily member COG0412:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.19  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491853662 240 VDYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDSRFKVVISNDSGCGGAALSKRVygeniARITtvlshwfCPAFSQYA 319
Cdd:COG0412   97 LDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADDLLDLA-----ARIK-------APVLLLYG 164

                         90
                 ....*....|....*
gi 491853662 320 GNEENLPFDQHEMLA 334
Cdd:COG0412  165 EKDPLVPPEQVAALE 179
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
240-281 2.47e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.39  E-value: 2.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491853662 240 VDYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDS-RFKVVIS 281
Cdd:COG1506   81 IDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPdRFKAAVA 123
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
240-334 6.12e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.19  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491853662 240 VDYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDSRFKVVISNDSGCGGAALSKRVygeniARITtvlshwfCPAFSQYA 319
Cdd:COG0412   97 LDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADDLLDLA-----ARIK-------APVLLLYG 164

                         90
                 ....*....|....*
gi 491853662 320 GNEENLPFDQHEMLA 334
Cdd:COG0412  165 EKDPLVPPEQVAALE 179
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
 241-283 1.11e-03

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 40.89  E-value: 1.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 491853662  241 DYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDSRFKVVISND 283
Cdd:pfam03403 210 DWQQLKGNLDMSKIAVIGHSFGGATVIQSLSEDTRFRCGIALD 252
PLN00021 PLN00021
chlorophyllase
 216-266 7.07e-03

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 38.11  E-value: 7.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491853662 216 YISGSKNHDEWE-AIGVWAWGSSRIVDYLEREGRIDMSKIAIMGHSRQGKAA 266
Cdd:PLN00021  89 TLAGPDGTDEIKdAAAVINWLSSGLAAVLPEGVRPDLSKLALAGHSRGGKTA 140
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
240-281 2.47e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.39  E-value: 2.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491853662 240 VDYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDS-RFKVVIS 281
Cdd:COG1506   81 IDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPdRFKAAVA 123
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
240-334 6.12e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.19  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491853662 240 VDYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDSRFKVVISNDSGCGGAALSKRVygeniARITtvlshwfCPAFSQYA 319
Cdd:COG0412   97 LDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADDLLDLA-----ARIK-------APVLLLYG 164

                         90
                 ....*....|....*
gi 491853662 320 GNEENLPFDQHEMLA 334
Cdd:COG0412  165 EKDPLVPPEQVAALE 179
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
237-322 6.83e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 41.63  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491853662 237 SRIVDYLERE--------GRIDMSKIAIMGHSRQGKAALW-SGAQ--DSRFKVV--ISNDSGCGGAALSKRVYGENIARI 303
Cdd:COG4188  129 SFVLDQLLALnksdpplaGRLDLDRIGVIGHSLGGYTALAlAGARldFAALRQYcgKNPDLQCRALDLPRLAYDLRDPRI 208

                         90
                 ....*....|....*....
gi 491853662 304 TTVLShwFCPAFSQYAGNE 322
Cdd:COG4188  209 KAVVA--LAPGGSGLFGEE 225
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
 241-283 1.11e-03

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 40.89  E-value: 1.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 491853662  241 DYLEREGRIDMSKIAIMGHSRQGKAALWSGAQDSRFKVVISND 283
Cdd:pfam03403 210 DWQQLKGNLDMSKIAVIGHSFGGATVIQSLSEDTRFRCGIALD 252
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
240-281 5.49e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 37.98  E-value: 5.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 491853662  240 VDYLEREGRIDMSKIAIMGHSRQGKAALWS-GAQDSRFKVVIS 281
Cdd:pfam00326  52 AEYLIEQGYTDPDRLAIWGGSYGGYLTGAAlNQRPDLFKAAVA 94
PLN00021 PLN00021
chlorophyllase
 216-266 7.07e-03

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 38.11  E-value: 7.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491853662 216 YISGSKNHDEWE-AIGVWAWGSSRIVDYLEREGRIDMSKIAIMGHSRQGKAA 266
Cdd:PLN00021  89 TLAGPDGTDEIKdAAAVINWLSSGLAAVLPEGVRPDLSKLALAGHSRGGKTA 140
 
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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