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Conserved domains on  [gi|1006543555|ref|WP_061794044|]
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disulfide oxidoreductase [Cytobacillus firmus]

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
8-141 5.75e-76

disulfide bond formation protein B; Provisional


The actual alignment was detected with superfamily member PRK03113:

Pssm-ID: 469857  Cd Length: 139  Bit Score: 222.27  E-value: 5.75e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555   8 RRENLLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRISLYTMVLSAVGAGISIYHYS 87
Cdd:PRK03113    6 KQENALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSLPISSIGACISLYHYA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1006543555  88 IQKISFMADHAAACGRVPCTGQYINWLGFVTIPFLALTAFIIIFICSYLVWKKT 141
Cdd:PRK03113   86 IQKIPFFSAAAASCGRVPCTGEYINWFGFVTIPFLALIAFITIAVCSFIVIKNK 139
 
Name Accession Description Interval E-value
PRK03113 PRK03113
putative disulfide oxidoreductase; Provisional
8-141 5.75e-76

putative disulfide oxidoreductase; Provisional


Pssm-ID: 179540  Cd Length: 139  Bit Score: 222.27  E-value: 5.75e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555   8 RRENLLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRISLYTMVLSAVGAGISIYHYS 87
Cdd:PRK03113    6 KQENALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSLPISSIGACISLYHYA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1006543555  88 IQKISFMADHAAACGRVPCTGQYINWLGFVTIPFLALTAFIIIFICSYLVWKKT 141
Cdd:PRK03113   86 IQKIPFFSAAAASCGRVPCTGEYINWFGFVTIPFLALIAFITIAVCSFIVIKNK 139
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
8-138 1.28e-29

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 104.97  E-value: 1.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555   8 RRENLLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRIS----LYTMVLSAVGAGISI 83
Cdd:COG1495     2 SGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLrlllLLALLLALAGAGLAA 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1006543555  84 YHYSIQKISFMADHAAAC-----------------GRVPCTGQYINWLGfVTIPFLALTAFIIIFICSYLVW 138
Cdd:COG1495    82 YHVGLQWGPWPGPPSCGCgleyfpswpdwlpslfaGTGDCDEVQWTFLG-LSMPGWNLIAFALLALLALLAL 152
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
12-89 2.84e-11

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: 57.63  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555  12 LLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRISLYTMVL----SAVGAGISIYHYS 87
Cdd:pfam02600   4 LWLLLALASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLALLAALAPRRRLRRLLLLLallsALGGAGLAAYHVG 83

                  ..
gi 1006543555  88 IQ 89
Cdd:pfam02600  84 VQ 85
 
Name Accession Description Interval E-value
PRK03113 PRK03113
putative disulfide oxidoreductase; Provisional
8-141 5.75e-76

putative disulfide oxidoreductase; Provisional


Pssm-ID: 179540  Cd Length: 139  Bit Score: 222.27  E-value: 5.75e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555   8 RRENLLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRISLYTMVLSAVGAGISIYHYS 87
Cdd:PRK03113    6 KQENALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSLPISSIGACISLYHYA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1006543555  88 IQKISFMADHAAACGRVPCTGQYINWLGFVTIPFLALTAFIIIFICSYLVWKKT 141
Cdd:PRK03113   86 IQKIPFFSAAAASCGRVPCTGEYINWFGFVTIPFLALIAFITIAVCSFIVIKNK 139
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
8-138 1.28e-29

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 104.97  E-value: 1.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555   8 RRENLLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRIS----LYTMVLSAVGAGISI 83
Cdd:COG1495     2 SGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLrlllLLALLLALAGAGLAA 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1006543555  84 YHYSIQKISFMADHAAAC-----------------GRVPCTGQYINWLGfVTIPFLALTAFIIIFICSYLVW 138
Cdd:COG1495    82 YHVGLQWGPWPGPPSCGCgleyfpswpdwlpslfaGTGDCDEVQWTFLG-LSMPGWNLIAFALLALLALLAL 152
PRK00611 PRK00611
putative disulfide oxidoreductase; Provisional
9-130 7.80e-21

putative disulfide oxidoreductase; Provisional


Pssm-ID: 100616  Cd Length: 135  Bit Score: 82.15  E-value: 7.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555   9 RENLLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRISLYTMVLSAVGAGISIYHYSI 88
Cdd:PRK00611    6 RSYALYFAWLISCIGTLMSIYYSYILNVEPCVLCYYQRICLFPLVVILGIAAYREDSSIKIYALPLALVGFGIAIYQVCL 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1006543555  89 QKISFMAdhAAACGRVPCTGQyINWLGFVTIPFLALTAFIII 130
Cdd:PRK00611   86 QEIPGMT--LDICGRVSCSTK-LFLFGFITMPMASAAAFCAI 124
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
12-89 2.84e-11

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: 57.63  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555  12 LLFIAWAASILAMFGSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRISLYTMVL----SAVGAGISIYHYS 87
Cdd:pfam02600   4 LWLLLALASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLALLAALAPRRRLRRLLLLLallsALGGAGLAAYHVG 83

                  ..
gi 1006543555  88 IQ 89
Cdd:pfam02600  84 VQ 85
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
8-132 1.74e-03

disulfide bond formation protein B; Provisional


Pssm-ID: 235002  Cd Length: 169  Bit Score: 36.58  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006543555   8 RRENLLFIAWAASILAMF-GSLYFSEIRQYEPCELCWYQRIVMYPFAVVLGLAVVKKDYRiSLYTM----VLSAV-GAGI 81
Cdd:PRK02110    9 RRERRLLVLLGLICLALVgGALYLQYVKGEDPCPLCIIQRYAFLLIAIFAFLAAAMRNTR-GVWVLegliVLSALgGIAV 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1006543555  82 SIYHYSIQkisfmADHAAACGRVP-----------------------CTGQYINWLGfVTIPFLALTAFIIIFI 132
Cdd:PRK02110   88 AGRHVYIQ-----LNPGFSCGIDAlqpivdslppakwlpgvfkvdglCETPYPPILG-LSLPGWALIAFVLIAV 155
 
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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