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Conserved domains on  [gi|515332397|ref|WP_016856148|]
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disulfide bond formation protein B [Halomonas smyrnensis]

Protein Classification

disulfide bond formation protein B( domain architecture ID 10003930)

disulfide bond formation protein B catalyzes disulfide bond formation in some periplasmic proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
8-165 2.07e-40

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


:

Pssm-ID: 441104  Cd Length: 153  Bit Score: 133.86  E-value: 2.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   8 ARVRCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAALHdPKGRLGAALYGLLSLLAVGtGIG 87
Cdd:COG1495    1 SSGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALL-PPRRGLRLLLLLALLLALA-GAG 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515332397  88 LAGRHLWLQSLPADQVPTCGPGLDYMMEVlplQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALAPLGLMW 165
Cdd:COG1495   79 LAAYHVGLQWGPWPGPPSCGCGLEYFPSW---PDWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIAFALLALLALLALL 153
 
Name Accession Description Interval E-value
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
8-165 2.07e-40

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 133.86  E-value: 2.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   8 ARVRCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAALHdPKGRLGAALYGLLSLLAVGtGIG 87
Cdd:COG1495    1 SSGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALL-PPRRGLRLLLLLALLLALA-GAG 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515332397  88 LAGRHLWLQSLPADQVPTCGPGLDYMMEVlplQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALAPLGLMW 165
Cdd:COG1495   79 LAAYHVGLQWGPWPGPPSCGCGLEYFPSW---PDWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIAFALLALLALLALL 153
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
11-159 5.79e-39

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: 130.05  E-value: 5.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   11 RCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAAlHDPKGRLGAALYGLLSLLAVGtGIGLAG 90
Cdd:pfam02600   2 RLLWLLLALASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLALLAA-LAPRRRLRRLLLLLALLSALG-GAGLAA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515332397   91 RHLWLQSLPADQVpTCGPgLDYMMEVLPLQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALA 159
Cdd:pfam02600  80 YHVGVQLLPWPPA-SCSF-LEYFPEWLPLDKWLPALFKGTGDCDEVAWTFLGLSMAGWNLLIFALLALL 146
PRK04388 PRK04388
disulfide bond formation protein B; Provisional
9-167 1.44e-38

disulfide bond formation protein B; Provisional


Pssm-ID: 235294  Cd Length: 172  Bit Score: 129.96  E-value: 1.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   9 RVRCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAALHDPKGRLGAALYGLLSLLAVGTGIGL 88
Cdd:PRK04388   7 SFRAQFLLGFLACAGLLAYAIFVQLHLGLEPCPLCIFQRIAFAALALLFLIGALHGPRNAGGRKAYGVLAFIAAGVGMGI 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515332397  89 AGRHLWLQSLPADQVPTCGPGLDYMMEVLPLQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALAPLGLMWRA 167
Cdd:PRK04388  87 AARHVWVQIRPKDMMSSCGPPLSFLSETMGPFEVFRTVLTGTGDCGNIDWRFLGLSMPMWSMVWFVGLALWALYAGFKA 165
 
Name Accession Description Interval E-value
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
8-165 2.07e-40

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 133.86  E-value: 2.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   8 ARVRCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAALHdPKGRLGAALYGLLSLLAVGtGIG 87
Cdd:COG1495    1 SSGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALL-PPRRGLRLLLLLALLLALA-GAG 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515332397  88 LAGRHLWLQSLPADQVPTCGPGLDYMMEVlplQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALAPLGLMW 165
Cdd:COG1495   79 LAAYHVGLQWGPWPGPPSCGCGLEYFPSW---PDWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIAFALLALLALLALL 153
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
11-159 5.79e-39

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: 130.05  E-value: 5.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   11 RCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAAlHDPKGRLGAALYGLLSLLAVGtGIGLAG 90
Cdd:pfam02600   2 RLLWLLLALASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLALLAA-LAPRRRLRRLLLLLALLSALG-GAGLAA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515332397   91 RHLWLQSLPADQVpTCGPgLDYMMEVLPLQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALA 159
Cdd:pfam02600  80 YHVGVQLLPWPPA-SCSF-LEYFPEWLPLDKWLPALFKGTGDCDEVAWTFLGLSMAGWNLLIFALLALL 146
PRK04388 PRK04388
disulfide bond formation protein B; Provisional
9-167 1.44e-38

disulfide bond formation protein B; Provisional


Pssm-ID: 235294  Cd Length: 172  Bit Score: 129.96  E-value: 1.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   9 RVRCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAALHDPKGRLGAALYGLLSLLAVGTGIGL 88
Cdd:PRK04388   7 SFRAQFLLGFLACAGLLAYAIFVQLHLGLEPCPLCIFQRIAFAALALLFLIGALHGPRNAGGRKAYGVLAFIAAGVGMGI 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515332397  89 AGRHLWLQSLPADQVPTCGPGLDYMMEVLPLQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALAPLGLMWRA 167
Cdd:PRK04388  87 AARHVWVQIRPKDMMSSCGPPLSFLSETMGPFEVFRTVLTGTGDCGNIDWRFLGLSMPMWSMVWFVGLALWALYAGFKA 165
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
1-166 5.71e-22

disulfide bond formation protein B; Provisional


Pssm-ID: 235002  Cd Length: 169  Bit Score: 87.04  E-value: 5.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397   1 MIETLREARVRCWSLAGLAFCVLMMAVALGLEHIGGLEPCPLCIFQRVAVISAGVVFAVAALHdpKGRLGAALYGLLSLL 80
Cdd:PRK02110   2 NNDTLMLRRERRLLVLLGLICLALVGGALYLQYVKGEDPCPLCIIQRYAFLLIAIFAFLAAAM--RNTRGVWVLEGLIVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397  81 AVGTGIGLAGRHLWLQSLPADqvpTCG-PGLDYMMEVLPLQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALA 159
Cdd:PRK02110  80 SALGGIAVAGRHVYIQLNPGF---SCGiDALQPIVDSLPPAKWLPGVFKVDGLCETPYPPILGLSLPGWALIAFVLIAVA 156

                 ....*..
gi 515332397 160 PLGLMWR 166
Cdd:PRK02110 157 VAVSLIR 163
PRK01749 PRK01749
disulfide bond formation protein DsbB;
13-159 9.18e-15

disulfide bond formation protein DsbB;


Pssm-ID: 234979  Cd Length: 176  Bit Score: 68.43  E-value: 9.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332397  13 WSLagLAFCVLMM-AVALGLEHIGGLEPCPLCIFQRVA---VISAGVVFAVAalhdPKGRLGAALYGLLSLLAVGTGIGL 88
Cdd:PRK01749  15 WLL--LAFTALALeLTALYFQHVMLLKPCVMCIYERVAlfgILGAGLIGAIA----PKTPLLRWLALLIWLYSAWKGLQL 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515332397  89 AGRHLWLQSLPADQVpTCgpglDYMMEV---LPLQQVVTMVLSASGECAEISARFLGLSLPGWTLIGFVVLALA 159
Cdd:PRK01749  89 ALEHTDYQLNPSPFN-TC----DFFVEFpswLPLDKWLPSVFVASGDCSERQWQFLGLEMPQWLVVIFAAYLVV 157
 
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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