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Conserved domains on  [gi|1267523260|ref|WP_098326617.1|]
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disulfide oxidoreductase

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
2-138 1.99e-66

disulfide bond formation protein B; Provisional


The actual alignment was detected with superfamily member PRK03113:

Pssm-ID: 469857  Cd Length: 139  Bit Score: 198.00  E-value: 1.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260   2 NSIEKKLDYILCSAWSVSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLLLGTAIIRKDYKIGIYSLIFSIVGACIA 81
Cdd:PRK03113    1 MGREKKQENALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSLPISSIGACIS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1267523260  82 TYHYLLQIIPFSLENAESCGRISCTEDYLDGFGFITIPFLALLAFLIIIICSFTLMK 138
Cdd:PRK03113   81 LYHYAIQKIPFFSAAAASCGRVPCTGEYINWFGFVTIPFLALIAFITIAVCSFIVIK 137
 
Name Accession Description Interval E-value
PRK03113 PRK03113
putative disulfide oxidoreductase; Provisional
2-138 1.99e-66

putative disulfide oxidoreductase; Provisional


Pssm-ID: 179540  Cd Length: 139  Bit Score: 198.00  E-value: 1.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260   2 NSIEKKLDYILCSAWSVSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLLLGTAIIRKDYKIGIYSLIFSIVGACIA 81
Cdd:PRK03113    1 MGREKKQENALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSLPISSIGACIS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1267523260  82 TYHYLLQIIPFSLENAESCGRISCTEDYLDGFGFITIPFLALLAFLIIIICSFTLMK 138
Cdd:PRK03113   81 LYHYAIQKIPFFSAAAASCGRVPCTGEYINWFGFVTIPFLALIAFITIAVCSFIVIK 137
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
15-134 3.76e-27

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 98.81  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260  15 AWSVSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLLLGTAIIRKDYKIG----IYSLIFSIVGACIATYHYLLQII 90
Cdd:COG1495    10 LALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLrlllLLALLLALAGAGLAAYHVGLQWG 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267523260  91 PFSLENAESC-----------------GRISCTEDYLDGFGfITIPFLALLAFLIIIICSF 134
Cdd:COG1495    90 PWPGPPSCGCgleyfpswpdwlpslfaGTGDCDEVQWTFLG-LSMPGWNLIAFALLALLAL 149
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
18-134 5.06e-10

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: 54.16  E-value: 5.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260  18 VSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLL-LGTAIIRKDYKIGIYSLI---FSIVGACIATYHYLLQIIPFS 93
Cdd:pfam02600  11 ASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLaLLAALAPRRRLRRLLLLLallSALGGAGLAAYHVGVQLLPWP 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267523260  94 lenAESCGRI---------------------SCTEDYLDGFGfITIPFLALLAFLIIIICSF 134
Cdd:pfam02600  91 ---PASCSFLeyfpewlpldkwlpalfkgtgDCDEVAWTFLG-LSMAGWNLLIFALLALLAL 148
 
Name Accession Description Interval E-value
PRK03113 PRK03113
putative disulfide oxidoreductase; Provisional
2-138 1.99e-66

putative disulfide oxidoreductase; Provisional


Pssm-ID: 179540  Cd Length: 139  Bit Score: 198.00  E-value: 1.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260   2 NSIEKKLDYILCSAWSVSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLLLGTAIIRKDYKIGIYSLIFSIVGACIA 81
Cdd:PRK03113    1 MGREKKQENALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSLPISSIGACIS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1267523260  82 TYHYLLQIIPFSLENAESCGRISCTEDYLDGFGFITIPFLALLAFLIIIICSFTLMK 138
Cdd:PRK03113   81 LYHYAIQKIPFFSAAAASCGRVPCTGEYINWFGFVTIPFLALIAFITIAVCSFIVIK 137
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
15-134 3.76e-27

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 98.81  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260  15 AWSVSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLLLGTAIIRKDYKIG----IYSLIFSIVGACIATYHYLLQII 90
Cdd:COG1495    10 LALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLrlllLLALLLALAGAGLAAYHVGLQWG 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267523260  91 PFSLENAESC-----------------GRISCTEDYLDGFGfITIPFLALLAFLIIIICSF 134
Cdd:COG1495    90 PWPGPPSCGCgleyfpswpdwlpslfaGTGDCDEVQWTFLG-LSMPGWNLIAFALLALLAL 149
PRK00611 PRK00611
putative disulfide oxidoreductase; Provisional
9-129 2.61e-20

putative disulfide oxidoreductase; Provisional


Pssm-ID: 100616  Cd Length: 135  Bit Score: 80.61  E-value: 2.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260   9 DYILCSAWSVSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLLLGTAIIRKDYKIGIYSLIFSIVGACIATYHYLLQ 88
Cdd:PRK00611    7 SYALYFAWLISCIGTLMSIYYSYILNVEPCVLCYYQRICLFPLVVILGIAAYREDSSIKIYALPLALVGFGIAIYQVCLQ 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1267523260  89 IIPFSleNAESCGRISCTEDyLDGFGFITIPFLALLAFLII 129
Cdd:PRK00611   87 EIPGM--TLDICGRVSCSTK-LFLFGFITMPMASAAAFCAI 124
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
18-134 5.06e-10

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: 54.16  E-value: 5.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260  18 VSFVATLGSLYLSEIMKYEPCTLCWYQRILMYPLVLL-LGTAIIRKDYKIGIYSLI---FSIVGACIATYHYLLQIIPFS 93
Cdd:pfam02600  11 ASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLaLLAALAPRRRLRRLLLLLallSALGGAGLAAYHVGVQLLPWP 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267523260  94 lenAESCGRI---------------------SCTEDYLDGFGfITIPFLALLAFLIIIICSF 134
Cdd:pfam02600  91 ---PASCSFLeyfpewlpldkwlpalfkgtgDCDEVAWTFLG-LSMAGWNLLIFALLALLAL 148
PRK04388 PRK04388
disulfide bond formation protein B; Provisional
26-101 4.74e-03

disulfide bond formation protein B; Provisional


Pssm-ID: 235294  Cd Length: 172  Bit Score: 35.58  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267523260  26 SLYLSEIMKYEPCTLCWYQRILMYPLVLLLGTAII--------RKDYkiGIYSLIFSIVGACIATYHYLLQIIPFslENA 97
Cdd:PRK04388   26 AIFVQLHLGLEPCPLCIFQRIAFAALALLFLIGALhgprnaggRKAY--GVLAFIAAGVGMGIAARHVWVQIRPK--DMM 101

                  ....
gi 1267523260  98 ESCG 101
Cdd:PRK04388  102 SSCG 105
 
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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