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Conserved domains on  [gi|512744812|ref|WP_016501489|]
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MULTISPECIES: WbuC family cupin fold metalloprotein [Pseudomonas]

Protein Classification

WbuC family cupin fold metalloprotein( domain architecture ID 10025083)

WbuC family cupin fold metalloprotein contains the conserved His residues that serve as metal-binding ligands

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_WbuC TIGR04366
cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to ...
 6-138 3.32e-61

cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to cupin fold proteins (see pfam07883), including conserved His residues likely to serve as metal-binding ligands. Many members occur in bacterial O-antigen biosynthesis regions. Some members have acquired the gene symbol wbuC (e.g. Jarvis, et al, 2011), but publications using this term do not ascribe a function.


:

Pssm-ID: 275159  Cd Length: 132  Bit Score: 185.07  E-value: 3.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512744812    6 FIDQSLFAGLAEKAAANPRGRQHHSFHE-MEEPCHRMAVGLQPSTYIPPHRHLsdDKAEALIVLKGRLGLLIFDEQGAVT 84
Cdd:TIGR04366   1 LIDQELLDELKAQAAKSPRLRANLNLHPsLDDPVQRMLIALEPGTYVRPHRHP--HKSETFIVLEGELDVLLFDDDGEVT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 512744812   85 DKRVLQAGGDCLGVDLAPGTYHGLVVLEPDSILFECKAGPYRPVGEGEHAQWAP 138
Cdd:TIGR04366  79 ERVVLSPGGGTFGVEIPPGTWHTLVALSEGTVIFEVKEGPYDPLADKDFAPWAP 132
 
Name Accession Description Interval E-value
cupin_WbuC TIGR04366
cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to ...
 6-138 3.32e-61

cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to cupin fold proteins (see pfam07883), including conserved His residues likely to serve as metal-binding ligands. Many members occur in bacterial O-antigen biosynthesis regions. Some members have acquired the gene symbol wbuC (e.g. Jarvis, et al, 2011), but publications using this term do not ascribe a function.


Pssm-ID: 275159  Cd Length: 132  Bit Score: 185.07  E-value: 3.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512744812    6 FIDQSLFAGLAEKAAANPRGRQHHSFHE-MEEPCHRMAVGLQPSTYIPPHRHLsdDKAEALIVLKGRLGLLIFDEQGAVT 84
Cdd:TIGR04366   1 LIDQELLDELKAQAAKSPRLRANLNLHPsLDDPVQRMLIALEPGTYVRPHRHP--HKSETFIVLEGELDVLLFDDDGEVT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 512744812   85 DKRVLQAGGDCLGVDLAPGTYHGLVVLEPDSILFECKAGPYRPVGEGEHAQWAP 138
Cdd:TIGR04366  79 ERVVLSPGGGTFGVEIPPGTWHTLVALSEGTVIFEVKEGPYDPLADKDFAPWAP 132
cupin_WbuC-like cd07005
Escherichia coli WbuC and related proteins, cupin domain; This family includes bacterial ...
 24-136 3.38e-56

Escherichia coli WbuC and related proteins, cupin domain; This family includes bacterial proteins homologous to WbuC, an Escherichia coli protein of unknown function with a cupin beta barrel fold. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380408  Cd Length: 114  Bit Score: 171.55  E-value: 3.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512744812  24 RGRQHHSFHE-MEEPCHRMAVGLQPSTYIPPHRHLSDDKAEALIVLKGRLGLLIFDEQGAVTDKRVLQAGGDCLGVDLAP 102
Cdd:cd07005    1 RRRAHLNLHEsPDDPVQRMLNALQPGTYVRPHRHPDPPKWELFVVLRGRIAVLIFDDDGTVTERVILGAGGGVFGIEIPP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 512744812 103 GTYHGLVVLEPDSILFECKAGPYRPVGEGEHAQW 136
Cdd:cd07005   81 GTWHTVVALEPDTVIFEVKEGPYDPATDKDFAPW 114
DUF6016 pfam19480
Domain of unknown function (DUF6016); This presumed domain is related to proteins in the Cupin ...
 7-125 5.88e-13

Domain of unknown function (DUF6016); This presumed domain is related to proteins in the Cupin superfamily. These proteins contain 1 or 2 copies of the domain. This family of proteins is found in Proteobacteria and Bacteroidetes. Proteins in this family are typically between 132 and 162 amino acids in length.


Pssm-ID: 437312  Cd Length: 141  Bit Score: 62.30  E-value: 5.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512744812    7 IDQSLFAGLAEKAAANPRGRQHHSFHEME-EPCHRMAVGLQPSTYIPPHRHlsDDKAEALIVLKGRLGLLIFDEQGAVTD 85
Cdd:pfam19480   1 LNKEFLGKLFEQAMANPRLRQNFDLRTSEaDTSQRMLNALLPGTVVPIHRH--EDTTESVLCLCGKLDEVIYEEVGAYAE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512744812   86 KRV-LQAGGDC-----------------------LGVDLAPGTYHGLVVLEPdSILFECKAGPY 125
Cdd:pfam19480  79 EAAaFPMGMDAqevtrkkefrevqrihlcpaegnYGCQIPQGAWHTVEVLEP-SVIFEAKDGAY 141
 
Name Accession Description Interval E-value
cupin_WbuC TIGR04366
cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to ...
 6-138 3.32e-61

cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to cupin fold proteins (see pfam07883), including conserved His residues likely to serve as metal-binding ligands. Many members occur in bacterial O-antigen biosynthesis regions. Some members have acquired the gene symbol wbuC (e.g. Jarvis, et al, 2011), but publications using this term do not ascribe a function.


Pssm-ID: 275159  Cd Length: 132  Bit Score: 185.07  E-value: 3.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512744812    6 FIDQSLFAGLAEKAAANPRGRQHHSFHE-MEEPCHRMAVGLQPSTYIPPHRHLsdDKAEALIVLKGRLGLLIFDEQGAVT 84
Cdd:TIGR04366   1 LIDQELLDELKAQAAKSPRLRANLNLHPsLDDPVQRMLIALEPGTYVRPHRHP--HKSETFIVLEGELDVLLFDDDGEVT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 512744812   85 DKRVLQAGGDCLGVDLAPGTYHGLVVLEPDSILFECKAGPYRPVGEGEHAQWAP 138
Cdd:TIGR04366  79 ERVVLSPGGGTFGVEIPPGTWHTLVALSEGTVIFEVKEGPYDPLADKDFAPWAP 132
cupin_WbuC-like cd07005
Escherichia coli WbuC and related proteins, cupin domain; This family includes bacterial ...
 24-136 3.38e-56

Escherichia coli WbuC and related proteins, cupin domain; This family includes bacterial proteins homologous to WbuC, an Escherichia coli protein of unknown function with a cupin beta barrel fold. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380408  Cd Length: 114  Bit Score: 171.55  E-value: 3.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512744812  24 RGRQHHSFHE-MEEPCHRMAVGLQPSTYIPPHRHLSDDKAEALIVLKGRLGLLIFDEQGAVTDKRVLQAGGDCLGVDLAP 102
Cdd:cd07005    1 RRRAHLNLHEsPDDPVQRMLNALQPGTYVRPHRHPDPPKWELFVVLRGRIAVLIFDDDGTVTERVILGAGGGVFGIEIPP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 512744812 103 GTYHGLVVLEPDSILFECKAGPYRPVGEGEHAQW 136
Cdd:cd07005   81 GTWHTVVALEPDTVIFEVKEGPYDPATDKDFAPW 114
DUF6016 pfam19480
Domain of unknown function (DUF6016); This presumed domain is related to proteins in the Cupin ...
 7-125 5.88e-13

Domain of unknown function (DUF6016); This presumed domain is related to proteins in the Cupin superfamily. These proteins contain 1 or 2 copies of the domain. This family of proteins is found in Proteobacteria and Bacteroidetes. Proteins in this family are typically between 132 and 162 amino acids in length.


Pssm-ID: 437312  Cd Length: 141  Bit Score: 62.30  E-value: 5.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512744812    7 IDQSLFAGLAEKAAANPRGRQHHSFHEME-EPCHRMAVGLQPSTYIPPHRHlsDDKAEALIVLKGRLGLLIFDEQGAVTD 85
Cdd:pfam19480   1 LNKEFLGKLFEQAMANPRLRQNFDLRTSEaDTSQRMLNALLPGTVVPIHRH--EDTTESVLCLCGKLDEVIYEEVGAYAE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512744812   86 KRV-LQAGGDC-----------------------LGVDLAPGTYHGLVVLEPdSILFECKAGPY 125
Cdd:pfam19480  79 EAAaFPMGMDAqevtrkkefrevqrihlcpaegnYGCQIPQGAWHTVEVLEP-SVIFEAKDGAY 141
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 47-115 1.98e-03

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 35.97  E-value: 1.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512744812  47 PSTYIPPHRHLSDDkaEALIVLKGRLGLLIFDEqgavtdKRVLQAGgdclgvDLA---PGTYHGLVVLEPDS 115
Cdd:cd02215   41 KGDAIPPHYHKRHH--ETFYVLEGRLQLWLDGE------SRLLTPG------DFAsvpPGTIHAYRMLSPDT 98
 
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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