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Conserved domains on  [gi|2793107673|ref|WP_371918557|]
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disulfide bond formation protein B, partial [Pseudomonas sp. GW456-E6]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02110 super family cl00649
disulfide bond formation protein B; Provisional
 5-35 2.25e-04

disulfide bond formation protein B; Provisional


The actual alignment was detected with superfamily member PRK02110:

Pssm-ID: 469857  Cd Length: 169  Bit Score: 36.58  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2793107673   5 IGVLAGGFIVQFGLHEFPCPLCMLQRYSMML 35
Cdd:PRK02110   23 LALVGGALYLQYVKGEDPCPLCIIQRYAFLL 53
 
Name Accession Description Interval E-value
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
 5-35 2.25e-04

disulfide bond formation protein B; Provisional


Pssm-ID: 235002  Cd Length: 169  Bit Score: 36.58  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2793107673   5 IGVLAGGFIVQFGLHEFPCPLCMLQRYSMML 35
Cdd:PRK02110   23 LALVGGALYLQYVKGEDPCPLCIIQRYAFLL 53
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
 2-36 4.09e-04

Disulfide bond formation protein DsbB; This family consists of disulfide bond formation protein DsbB from bacteria. The DsbB protein oxidizes the periplasmic protein DsbA which in turn oxidizes cysteines in other periplasmic proteins in order to make disulfide bonds. DsbB acts as a redox potential transducer across the cytoplasmic membrane and is an integral membrane protein. DsbB posses six cysteines four of which are necessary for it proper function in vivo.


Pssm-ID: 460613  Cd Length: 149  Bit Score: 35.67  E-value: 4.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2793107673   2 LAYIGVLAGGFIVQFGLHEFPCPLCMLQRYSMMLA 36
Cdd:pfam02600  10 LASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAI 44
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
 5-36 7.34e-03

Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441104  Cd Length: 153  Bit Score: 32.55  E-value: 7.34e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2793107673   5 IGVLAGGFIVQFGLHEFPCPLCMLQRYSMMLA 36
Cdd:COG1495    15 LALLLGALYFQYVLGLEPCPLCIYQRIAMYGL 46
 
Name Accession Description Interval E-value
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
 5-35 2.25e-04

disulfide bond formation protein B; Provisional


Pssm-ID: 235002  Cd Length: 169  Bit Score: 36.58  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2793107673   5 IGVLAGGFIVQFGLHEFPCPLCMLQRYSMML 35
Cdd:PRK02110   23 LALVGGALYLQYVKGEDPCPLCIIQRYAFLL 53
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
 2-36 4.09e-04

Disulfide bond formation protein DsbB; This family consists of disulfide bond formation protein DsbB from bacteria. The DsbB protein oxidizes the periplasmic protein DsbA which in turn oxidizes cysteines in other periplasmic proteins in order to make disulfide bonds. DsbB acts as a redox potential transducer across the cytoplasmic membrane and is an integral membrane protein. DsbB posses six cysteines four of which are necessary for it proper function in vivo.


Pssm-ID: 460613  Cd Length: 149  Bit Score: 35.67  E-value: 4.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2793107673   2 LAYIGVLAGGFIVQFGLHEFPCPLCMLQRYSMMLA 36
Cdd:pfam02600  10 LASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAI 44
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
 5-36 7.34e-03

Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441104  Cd Length: 153  Bit Score: 32.55  E-value: 7.34e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2793107673   5 IGVLAGGFIVQFGLHEFPCPLCMLQRYSMMLA 36
Cdd:COG1495    15 LALLLGALYFQYVLGLEPCPLCIYQRIAMYGL 46
 
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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