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Conserved domains on  [gi|496079392|ref|WP_008803899|]
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MULTISPECIES: WbuC family cupin fold metalloprotein [Klebsiella]

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 ...
 3-132 3.26e-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: 3.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392    3 QITLSDMQQQSEAAASAPRLRAHRNFHPELSDPVQRLAIAMEPGTYIRPHRHRHTFELLLPLKGRFVVLNFDDNGVVTRR 82
Cdd:TIGR04366   1 LIDQELLDELKAQAAKSPRLRANLNLHPSLDDPVQRMLIALEPGTYVRPHRHPHKSETFIVLEGELDVLLFDDDGEVTER 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496079392   83 VVLG--ETCTALEMEAGTWHTVLSLDPGGMVFEVKQGAYQPLAEVDTMAWAP 132
Cdd:TIGR04366  81 VVLSpgGGTFGVEIPPGTWHTLVALSEGTVIFEVKEGPYDPLADKDFAPWAP 132
 
Name Accession Description Interval E-value
cupin_WbuC TIGR04366
cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to ...
 3-132 3.26e-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: 3.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392    3 QITLSDMQQQSEAAASAPRLRAHRNFHPELSDPVQRLAIAMEPGTYIRPHRHRHTFELLLPLKGRFVVLNFDDNGVVTRR 82
Cdd:TIGR04366   1 LIDQELLDELKAQAAKSPRLRANLNLHPSLDDPVQRMLIALEPGTYVRPHRHPHKSETFIVLEGELDVLLFDDDGEVTER 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496079392   83 VVLG--ETCTALEMEAGTWHTVLSLDPGGMVFEVKQGAYQPLAEVDTMAWAP 132
Cdd:TIGR04366  81 VVLSpgGGTFGVEIPPGTWHTLVALSEGTVIFEVKEGPYDPLADKDFAPWAP 132
cupin_WbuC-like cd07005
Escherichia coli WbuC and related proteins, cupin domain; This family includes bacterial ...
 21-130 3.20e-55

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: 169.24  E-value: 3.20e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392  21 RLRAHRNFHPELSDPVQRLAIAMEPGTYIRPHRHR--HTFELLLPLKGRFVVLNFDDNGVVTRRVVLGET--CTALEMEA 96
Cdd:cd07005    1 RRRAHLNLHESPDDPVQRMLNALQPGTYVRPHRHPdpPKWELFVVLRGRIAVLIFDDDGTVTERVILGAGggVFGIEIPP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 496079392  97 GTWHTVLSLDPGGMVFEVKQGAYQPLAEVDTMAW 130
Cdd:cd07005   81 GTWHTVVALEPDTVIFEVKEGPYDPATDKDFAPW 114
DUF6016 pfam19480
Domain of unknown function (DUF6016); This presumed domain is related to proteins in the Cupin ...
 14-119 4.65e-12

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: 59.99  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392   14 EAAASAPRLRAHRNFHPELSDPVQRLAIAMEPGTYIRPHRHRHTFELLLPLKGRFVVLNFDDNGV--------------- 78
Cdd:pfam19480  11 EQAMANPRLRQNFDLRTSEADTSQRMLNALLPGTVVPIHRHEDTTESVLCLCGKLDEVIYEEVGAyaeeaaafpmgmdaq 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496079392   79 -VTRRVVLGET-----CTAL-----EMEAGTWHTVLSLDPgGMVFEVKQGAY 119
Cdd:pfam19480  91 eVTRKKEFREVqrihlCPAEgnygcQIPQGAWHTVEVLEP-SVIFEAKDGAY 141
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
41-121 1.57e-03

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 36.27  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392  41 IAMEPGTYIRPHRHRHTFELLLPLKGRFVVLnFDDngvvtRRVVLGEtCTALEMEAGTWHTVLSLDPGGMVF-EVKQGAY 119
Cdd:COG0662   32 ITVPPGAELSLHVHPHRDEFFYVLEGTGEVT-IGD-----EEVELKA-GDSVYIPAGVPHRLRNPGDEPLELlEVQAPAY 104


                 ..
gi 496079392 120 QP 121
Cdd:COG0662  105 LG 106
 
Name Accession Description Interval E-value
cupin_WbuC TIGR04366
cupin fold metalloprotein, WbuC family; Members of this family show sequence similarity to ...
 3-132 3.26e-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: 3.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392    3 QITLSDMQQQSEAAASAPRLRAHRNFHPELSDPVQRLAIAMEPGTYIRPHRHRHTFELLLPLKGRFVVLNFDDNGVVTRR 82
Cdd:TIGR04366   1 LIDQELLDELKAQAAKSPRLRANLNLHPSLDDPVQRMLIALEPGTYVRPHRHPHKSETFIVLEGELDVLLFDDDGEVTER 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496079392   83 VVLG--ETCTALEMEAGTWHTVLSLDPGGMVFEVKQGAYQPLAEVDTMAWAP 132
Cdd:TIGR04366  81 VVLSpgGGTFGVEIPPGTWHTLVALSEGTVIFEVKEGPYDPLADKDFAPWAP 132
cupin_WbuC-like cd07005
Escherichia coli WbuC and related proteins, cupin domain; This family includes bacterial ...
 21-130 3.20e-55

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: 169.24  E-value: 3.20e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392  21 RLRAHRNFHPELSDPVQRLAIAMEPGTYIRPHRHR--HTFELLLPLKGRFVVLNFDDNGVVTRRVVLGET--CTALEMEA 96
Cdd:cd07005    1 RRRAHLNLHESPDDPVQRMLNALQPGTYVRPHRHPdpPKWELFVVLRGRIAVLIFDDDGTVTERVILGAGggVFGIEIPP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 496079392  97 GTWHTVLSLDPGGMVFEVKQGAYQPLAEVDTMAW 130
Cdd:cd07005   81 GTWHTVVALEPDTVIFEVKEGPYDPATDKDFAPW 114
DUF6016 pfam19480
Domain of unknown function (DUF6016); This presumed domain is related to proteins in the Cupin ...
 14-119 4.65e-12

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: 59.99  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392   14 EAAASAPRLRAHRNFHPELSDPVQRLAIAMEPGTYIRPHRHRHTFELLLPLKGRFVVLNFDDNGV--------------- 78
Cdd:pfam19480  11 EQAMANPRLRQNFDLRTSEADTSQRMLNALLPGTVVPIHRHEDTTESVLCLCGKLDEVIYEEVGAyaeeaaafpmgmdaq 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496079392   79 -VTRRVVLGET-----CTAL-----EMEAGTWHTVLSLDPgGMVFEVKQGAY 119
Cdd:pfam19480  91 eVTRKKEFREVqrihlCPAEgnygcQIPQGAWHTVEVLEP-SVIFEAKDGAY 141
cupin_QdtA-like cd20292
sugar 3,4-ketoisomerase QdtA and related proteins, cupin domain; This family includes cupin ...
 52-108 2.22e-04

sugar 3,4-ketoisomerase QdtA and related proteins, cupin domain; This family includes cupin domains of several bacterial proteins homologous to sugar 3,4-ketoisomerases. Thermoanaerobacterium thermosaccharolyticum QdtA catalyzes a key step in the biosynthesis of these sugars, the conversion of thymidine diphosphate (dTDP)-4-keto-6-deoxyglucose to dTDP-3-keto-6-deoxyglucose. In Aneurinibacillus thermoaerophilus, TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase (also known as FdtA) is involved in the biosynthesis of dTDP-Fucp3NAc (3-acetamido-3,6-dideoxy-alpha-d-galactose), which is part of the repeating units of the glycan chain in the S-layer. Shewanella denitrificans bifunctional ketoisomerase/N-acetyltransferase (also known as FdtD) is involved in the third and fifth steps in the production of 3-acetamido-3,6-dideoxy-alpha-d-galactose or Fuc3NAc; the C-terminal cupin domain harbors the active site responsible for the isomerization reaction. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380426  Cd Length: 117  Bit Score: 38.61  E-value: 2.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496079392  52 HRHRHTFELLLPLKGRFVVLnfDDNGVVTRRVVLGETCTALEMEAGTWHTVLSLDPG 108
Cdd:cd20292   45 HAHKKLEQLLICLSGSCEVI--LDDGKEKEEFVLDSPNKGLYIPPGVWHEMYDFSPD 99
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
41-121 1.57e-03

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 36.27  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392  41 IAMEPGTYIRPHRHRHTFELLLPLKGRFVVLnFDDngvvtRRVVLGEtCTALEMEAGTWHTVLSLDPGGMVF-EVKQGAY 119
Cdd:COG0662   32 ITVPPGAELSLHVHPHRDEFFYVLEGTGEVT-IGD-----EEVELKA-GDSVYIPAGVPHRLRNPGDEPLELlEVQAPAY 104


                 ..
gi 496079392 120 QP 121
Cdd:COG0662  105 LG 106
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 43-112 1.99e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 35.31  E-value: 1.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496079392   43 MEPGTYIRPHRHRHTFELLLPLKGRfVVLNFDDngvvtRRVVLGETCtALEMEAGTWHTVLSLDPGGMVF 112
Cdd:pfam07883   5 LPPGESSPPHRHPGEDEFFYVLEGE-GELTVDG-----EEVVLKAGD-SVYFPAGVPHRFRNTGDEPARL 67
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 44-112 2.86e-03

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 34.77  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496079392  44 EPGTYIRPHRHRHTFELLLPLKGRFVVLNFDDngvvtRRVVLGETCTALeMEAGTWHTVLSLDPGGMVF 112
Cdd:cd02208    7 PPGTSSPPHWHPEQDEIFYVLSGEGELTLDDG-----ETVELKAGDIVL-IPPGVPHSFVNTSDEPAVF 69
 
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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