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Conserved domains on  [gi|647612132|ref|WP_025887754|]
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disulfide bond formation protein DsbB [Shewanella algae]

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
1-169 3.08e-74

disulfide bond formation protein B; Provisional


The actual alignment was detected with superfamily member PRK01749:

Pssm-ID: 469857  Cd Length: 176  Bit Score: 220.20  E-value: 3.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132   1 MTAMIRFAHSRMAWGILALSALSLELAALYFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSVRPVRLVAALLWGGS 80
Cdd:PRK01749   2 LRFLNQCSQGRGAWLLLAFTALALELTALYFQHVMLLKPCVMCIYERVALFGILGAGLIGAIAPKTPLLRWLALLIWLYS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  81 ASWGLRLAIELNDMQQNPSPFSTCSFLPDFPSWMPLHEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLLY 160
Cdd:PRK01749  82 AWKGLQLALEHTDYQLNPSPFNTCDFFVEFPSWLPLDKWLPSVFVASGDCSERQWQFLGLEMPQWLVVIFAAYLVVAVLV 161

                 ....*....
gi 647612132 161 VVPILSKGR 169
Cdd:PRK01749 162 LISQFFKAK 170
 
Name Accession Description Interval E-value
PRK01749 PRK01749
disulfide bond formation protein DsbB;
1-169 3.08e-74

disulfide bond formation protein DsbB;


Pssm-ID: 234979  Cd Length: 176  Bit Score: 220.20  E-value: 3.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132   1 MTAMIRFAHSRMAWGILALSALSLELAALYFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSVRPVRLVAALLWGGS 80
Cdd:PRK01749   2 LRFLNQCSQGRGAWLLLAFTALALELTALYFQHVMLLKPCVMCIYERVALFGILGAGLIGAIAPKTPLLRWLALLIWLYS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  81 ASWGLRLAIELNDMQQNPSPFSTCSFLPDFPSWMPLHEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLLY 160
Cdd:PRK01749  82 AWKGLQLALEHTDYQLNPSPFNTCDFFVEFPSWLPLDKWLPSVFVASGDCSERQWQFLGLEMPQWLVVIFAAYLVVAVLV 161

                 ....*....
gi 647612132 161 VVPILSKGR 169
Cdd:PRK01749 162 LISQFFKAK 170
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
30-159 1.28e-40

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: 133.90  E-value: 1.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132   30 YFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSvRPVRLVAALLWGGSASWGLRLAIELNDMQQNPSPFSTCSFLPD 109
Cdd:pfam02600  21 YFQHVLGLEPCPLCIYQRLAYLAIGLLALLAALAPR-RRLRRLLLLLALLSALGGAGLAAYHVGVQLLPWPPASCSFLEY 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 647612132  110 FPSWMPLHEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLL 159
Cdd:pfam02600 100 FPEWLPLDKWLPALFKGTGDCDEVAWTFLGLSMAGWNLLIFALLALLALL 149
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
30-159 1.30e-30

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 108.44  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  30 YFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSVRPVRLVaALLWGGSASWGLRLAIELNDMQQNPSPF-STCSFLP 108
Cdd:COG1495   23 YFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLRLL-LLLALLLALAGAGLAAYHVGLQWGPWPGpPSCGCGL 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647612132 109 DFPSWMPlhEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLL 159
Cdd:COG1495  102 EYFPSWP--DWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIAFALLALLALL 150
 
Name Accession Description Interval E-value
PRK01749 PRK01749
disulfide bond formation protein DsbB;
1-169 3.08e-74

disulfide bond formation protein DsbB;


Pssm-ID: 234979  Cd Length: 176  Bit Score: 220.20  E-value: 3.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132   1 MTAMIRFAHSRMAWGILALSALSLELAALYFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSVRPVRLVAALLWGGS 80
Cdd:PRK01749   2 LRFLNQCSQGRGAWLLLAFTALALELTALYFQHVMLLKPCVMCIYERVALFGILGAGLIGAIAPKTPLLRWLALLIWLYS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  81 ASWGLRLAIELNDMQQNPSPFSTCSFLPDFPSWMPLHEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLLY 160
Cdd:PRK01749  82 AWKGLQLALEHTDYQLNPSPFNTCDFFVEFPSWLPLDKWLPSVFVASGDCSERQWQFLGLEMPQWLVVIFAAYLVVAVLV 161

                 ....*....
gi 647612132 161 VVPILSKGR 169
Cdd:PRK01749 162 LISQFFKAK 170
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
30-159 1.28e-40

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: 133.90  E-value: 1.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132   30 YFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSvRPVRLVAALLWGGSASWGLRLAIELNDMQQNPSPFSTCSFLPD 109
Cdd:pfam02600  21 YFQHVLGLEPCPLCIYQRLAYLAIGLLALLAALAPR-RRLRRLLLLLALLSALGGAGLAAYHVGVQLLPWPPASCSFLEY 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 647612132  110 FPSWMPLHEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLL 159
Cdd:pfam02600 100 FPEWLPLDKWLPALFKGTGDCDEVAWTFLGLSMAGWNLLIFALLALLALL 149
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
30-159 1.30e-30

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 108.44  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  30 YFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSVRPVRLVaALLWGGSASWGLRLAIELNDMQQNPSPF-STCSFLP 108
Cdd:COG1495   23 YFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLRLL-LLLALLLALAGAGLAAYHVGLQWGPWPGpPSCGCGL 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647612132 109 DFPSWMPlhEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLL 159
Cdd:COG1495  102 EYFPSWP--DWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIAFALLALLALL 150
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
30-159 3.86e-09

disulfide bond formation protein B; Provisional


Pssm-ID: 235002  Cd Length: 169  Bit Score: 52.76  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  30 YFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSVRPVRLVAALL----WGGSASWGLRLAIELNdmqqnpsPFSTCS 105
Cdd:PRK02110  31 YLQYVKGEDPCPLCIIQRYAFLLIAIFAFLAAAMRNTRGVWVLEGLIvlsaLGGIAVAGRHVYIQLN-------PGFSCG 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 647612132 106 FLPDFP--SWMPLHEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFATYLVALLL 159
Cdd:PRK02110 104 IDALQPivDSLPPAKWLPGVFKVDGLCETPYPPILGLSLPGWALIAFVLIAVAVAV 159
PRK04307 PRK04307
protein-disulfide oxidoreductase DsbI;
30-130 1.72e-07

protein-disulfide oxidoreductase DsbI;


Pssm-ID: 235276  Cd Length: 218  Bit Score: 48.97  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  30 YFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFLAPSVRPVRLVAALLWGGSASWGLRLAIELNDMQQ---NPSPF---ST 103
Cdd:PRK04307  43 FFQIYLYMAPCEQCVYIRFAMFVMAIGGVIAAINPKNIILKLIGYIAAFYGSILGIKFSIKLNGIHHavhNDDPLfgvQG 122
                         90       100
                 ....*....|....*....|....*..
gi 647612132 104 CSFLPDFPSWMPLHEWLPSIFMPTGMC 130
Cdd:PRK04307 123 CSTDPTFPFNLPLAEWAPEWFKPTGDC 149
PRK04388 PRK04388
disulfide bond formation protein B; Provisional
30-169 1.54e-06

disulfide bond formation protein B; Provisional


Pssm-ID: 235294  Cd Length: 172  Bit Score: 45.98  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647612132  30 YFQHVMQLEPCVMCIYQRLAVLGLLLAGIIGFL-APSVRPVRLVAALLWGGSASWGLRLAIELNDMQQNP-SPFSTC--- 104
Cdd:PRK04388  28 FVQLHLGLEPCPLCIFQRIAFAALALLFLIGALhGPRNAGGRKAYGVLAFIAAGVGMGIAARHVWVQIRPkDMMSSCgpp 107
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647612132 105 -SFLPDFpswMPLHEWLPSIFMPTGMCTDIPWSFIGITMSQWMIVAFAtyLVALLLYVVPILSKGR 169
Cdd:PRK04388 108 lSFLSET---MGPFEVFRTVLTGTGDCGNIDWRFLGLSMPMWSMVWFV--GLALWALYAGFKARRR 168
 
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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