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Conserved domains on  [gi|653594731|ref|WP_027607623|]
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MULTISPECIES: disulfide bond formation protein B [Pseudomonas]

Protein Classification

disulfide bond formation protein B( domain architecture ID 10011749)

disulfide bond formation protein B is required for disulfide bond formation in some periplasmic proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
1-166 1.05e-90

disulfide bond formation protein B; Provisional


:

Pssm-ID: 235002  Cd Length: 169  Bit Score: 261.53  E-value: 1.05e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   1 MSDELRLGRERRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGAAMRTKGALTLFEGLVVLSA 80
Cdd:PRK02110   2 NNDTLMLRRERRLLVLLGLICLALVGGALYLQYVKGEDPCPLCIIQRYAFLLIAIFAFLAAAMRNTRGVWVLEGLIVLSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731  81 LGGVAAAGHHVYTQFFPQVSCGVDVLQPIVDDLPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVILVPLGI 160
Cdd:PRK02110  82 LGGIAVAGRHVYIQLNPGFSCGIDALQPIVDSLPPAKWLPGVFKVDGLCETPYPPILGLSLPGWALIAFVLIAVAVAVSL 161

                 ....*.
gi 653594731 161 YRNRRH 166
Cdd:PRK02110 162 IRNRRR 167
 
Name Accession Description Interval E-value
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
1-166 1.05e-90

disulfide bond formation protein B; Provisional


Pssm-ID: 235002  Cd Length: 169  Bit Score: 261.53  E-value: 1.05e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   1 MSDELRLGRERRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGAAMRTKGALTLFEGLVVLSA 80
Cdd:PRK02110   2 NNDTLMLRRERRLLVLLGLICLALVGGALYLQYVKGEDPCPLCIIQRYAFLLIAIFAFLAAAMRNTRGVWVLEGLIVLSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731  81 LGGVAAAGHHVYTQFFPQVSCGVDVLQPIVDDLPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVILVPLGI 160
Cdd:PRK02110  82 LGGIAVAGRHVYIQLNPGFSCGIDALQPIVDSLPPAKWLPGVFKVDGLCETPYPPILGLSLPGWALIAFVLIAVAVAVSL 161

                 ....*.
gi 653594731 161 YRNRRH 166
Cdd:PRK02110 162 IRNRRR 167
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
11-156 7.42e-38

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: 126.58  E-value: 7.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   11 RRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGAAMRTKGALTLFEGLVVLSALGGVAAAGHH 90
Cdd:pfam02600   2 RLLWLLLALASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLALLAALAPRRRLRRLLLLLALLSALGGAGLAAYH 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653594731   91 VYTQ--FFPQVSCgvDVLQPIVDDLPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVILV 156
Cdd:pfam02600  82 VGVQllPWPPASC--SFLEYFPEWLPLDKWLPALFKGTGDCDEVAWTFLGLSMAGWNLLIFALLALLA 147
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
9-155 1.09e-30

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 108.44  E-value: 1.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   9 RERRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGAAMRTKGALTLFEGLVVLSALGGVAAAG 88
Cdd:COG1495    2 SGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLRLLLLLALLLALAGAGLAA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731  89 HHVYTQFFP---QVSCGVDVLQPIvddlPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVIL 155
Cdd:COG1495   82 YHVGLQWGPwpgPPSCGCGLEYFP----SWPDWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIAFALLALL 147
 
Name Accession Description Interval E-value
PRK02110 PRK02110
disulfide bond formation protein B; Provisional
1-166 1.05e-90

disulfide bond formation protein B; Provisional


Pssm-ID: 235002  Cd Length: 169  Bit Score: 261.53  E-value: 1.05e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   1 MSDELRLGRERRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGAAMRTKGALTLFEGLVVLSA 80
Cdd:PRK02110   2 NNDTLMLRRERRLLVLLGLICLALVGGALYLQYVKGEDPCPLCIIQRYAFLLIAIFAFLAAAMRNTRGVWVLEGLIVLSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731  81 LGGVAAAGHHVYTQFFPQVSCGVDVLQPIVDDLPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVILVPLGI 160
Cdd:PRK02110  82 LGGIAVAGRHVYIQLNPGFSCGIDALQPIVDSLPPAKWLPGVFKVDGLCETPYPPILGLSLPGWALIAFVLIAVAVAVSL 161

                 ....*.
gi 653594731 161 YRNRRH 166
Cdd:PRK02110 162 IRNRRR 167
DsbB pfam02600
Disulfide bond formation protein DsbB; This family consists of disulfide bond formation ...
11-156 7.42e-38

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: 126.58  E-value: 7.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   11 RRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGAAMRTKGALTLFEGLVVLSALGGVAAAGHH 90
Cdd:pfam02600   2 RLLWLLLALASLALLGGALYFQHVLGLEPCPLCIYQRLAYLAIGLLALLAALAPRRRLRRLLLLLALLSALGGAGLAAYH 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653594731   91 VYTQ--FFPQVSCgvDVLQPIVDDLPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVILV 156
Cdd:pfam02600  82 VGVQllPWPPASC--SFLEYFPEWLPLDKWLPALFKGTGDCDEVAWTFLGLSMAGWNLLIFALLALLA 147
DsbB COG1495
Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, ...
9-155 1.09e-30

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


Pssm-ID: 441104  Cd Length: 153  Bit Score: 108.44  E-value: 1.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   9 RERRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGAAMRTKGALTLFEGLVVLSALGGVAAAG 88
Cdd:COG1495    2 SGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLRLLLLLALLLALAGAGLAA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731  89 HHVYTQFFP---QVSCGVDVLQPIvddlPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVIL 155
Cdd:COG1495   82 YHVGLQWGPwpgPPSCGCGLEYFP----SWPDWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIAFALLALL 147
PRK04388 PRK04388
disulfide bond formation protein B; Provisional
16-167 3.11e-13

disulfide bond formation protein B; Provisional


Pssm-ID: 235294  Cd Length: 172  Bit Score: 64.09  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731  16 LLG-IICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGA--AMRTKGALTLFEGLVVLSALGGVAAAGHHVY 92
Cdd:PRK04388  13 LLGfLACAGLLAYAIFVQLHLGLEPCPLCIFQRIAFAALALLFLIGAlhGPRNAGGRKAYGVLAFIAAGVGMGIAARHVW 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653594731  93 TQFFPQ---VSCGvDVLQPIVDDLPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAFVLTVILVPLGIYRNRRHK 167
Cdd:PRK04388  93 VQIRPKdmmSSCG-PPLSFLSETMGPFEVFRTVLTGTGDCGNIDWRFLGLSMPMWSMVWFVGLALWALYAGFKARRRS 169
PRK01749 PRK01749
disulfide bond formation protein DsbB;
6-157 2.00e-12

disulfide bond formation protein DsbB;


Pssm-ID: 234979  Cd Length: 176  Bit Score: 61.88  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731   6 RLGRERRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIAIFAFIGaAMRTKGALTLFEGLVV--LSALGG 83
Cdd:PRK01749   7 QCSQGRGAWLLLAFTALALELTALYFQHVMLLKPCVMCIYERVALFGILGAGLIG-AIAPKTPLLRWLALLIwlYSAWKG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594731  84 VAAAGHHVYTQFFPQ--VSCgvDVLQPIVDDLPLAKVFPLGFQVDGFCSTPYPPVLGLSLAQWALVAF-----VLTVILV 156
Cdd:PRK01749  86 LQLALEHTDYQLNPSpfNTC--DFFVEFPSWLPLDKWLPSVFVASGDCSERQWQFLGLEMPQWLVVIFaaylvVAVLVLI 163

                 .
gi 653594731 157 P 157
Cdd:PRK01749 164 S 164
 
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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