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type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB [Aeromonas salmonicida]

Protein Classification

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB( domain architecture ID 10014381)

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system

CATH:  3.40.30.10
PubMed:  16321931|15558583|10049365|12074972

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-178 3.08e-96

conjugal transfer protein TrbB; Provisional


:

Pssm-ID: 237484  Cd Length: 181  Bit Score: 276.22  E-value: 3.08e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   1 MNTLRTVVLTSWLLCLSATASTWDDIARLDAAK-------AARQDTSAQTRAADHPPFRLSDGRAVRVENWKLVLFMQST 73
Cdd:PRK13728   1 MSLTKLLLVLLLLMATAVQASTRDEIERLWNPKgmaaqpaQPAADTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546  74 CSYCHQFDPVLKQISEQTGIAVFPYSLDGRGDAAFPAALPAGPDVMVEFFNNgLPIATPTVFLVNVNTIMTFPMFQGAVA 153
Cdd:PRK13728  81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQGATD 159

                        170       180
                 ....*....|....*....|....*
gi 500229546 154 ADVFMTRLDEVFQValsIGGRHATR 178
Cdd:PRK13728 160 AAGFMARMDTVLQM---YGGKKGAK 181
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-178 3.08e-96

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 276.22  E-value: 3.08e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   1 MNTLRTVVLTSWLLCLSATASTWDDIARLDAAK-------AARQDTSAQTRAADHPPFRLSDGRAVRVENWKLVLFMQST 73
Cdd:PRK13728   1 MSLTKLLLVLLLLMATAVQASTRDEIERLWNPKgmaaqpaQPAADTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546  74 CSYCHQFDPVLKQISEQTGIAVFPYSLDGRGDAAFPAALPAGPDVMVEFFNNgLPIATPTVFLVNVNTIMTFPMFQGAVA 153
Cdd:PRK13728  81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQGATD 159

                        170       180
                 ....*....|....*....|....*
gi 500229546 154 ADVFMTRLDEVFQValsIGGRHATR 178
Cdd:PRK13728 160 AAGFMARMDTVLQM---YGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 4-164 3.64e-51

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.


Pssm-ID: 131785  Cd Length: 153  Bit Score: 161.13  E-value: 3.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546    4 LRTVVLTSWLLCLSATASTWDDIARLDAAKA---ARQDTSAQtraadhppfrlsdGRAVRVENWKLVLFMQSTCSYCHQF 80
Cdd:TIGR02738   2 LRKLLIVLLLLAGLAQASTLDEITNLWAPPQgltAATDNAPQ-------------GRHANQDDYALVFFYQSTCPYCHQF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   81 DPVLKQISEQTGIAVFPYSLDGRGDAAFPAALPAGPDVMVEFFNNGLPIATPTVFLVNVNTIMTFPMFQGAVAADVFMTR 160
Cdd:TIGR02738  69 APVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNPRPVVTPATFLVNVNTRKAYPVLQGAVDEAELANR 148


                  ....
gi 500229546  161 LDEV 164
Cdd:TIGR02738 149 MDEI 152
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 62-161 1.05e-13

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 66.56  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   62 ENWKLVLFMQSTCSYCHQFDPVLKQISEQTGIAVFPYSLDGRGDAAFPAALPagpdvmveffNNGLPIA-----TPTVFL 136
Cdd:pfam13728 129 EEFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYRV----------DNGQAARlgvkrTPALFL 198

                          90       100
                  ....*....|....*....|....*
gi 500229546  137 VNVNTIMTFPMFQGAVAADVFMTRL 161
Cdd:pfam13728 199 VNPPSGDVVPVAAGVLSLDELEERI 223
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 40-164 5.20e-05

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 5.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546  40 SAQTRAADHPPFRLSDGRAVRVENWK----LVLFMQSTCSYCHQFDPVLKQISEQT-GIAVFPYSLDGRGDAA------- 107
Cdd:COG0526    2 KAVGKPAPDFTLTDLDGKPLSLADLKgkpvLVNFWATWCPPCRAEMPVLKELAEEYgGVVFVGVDVDENPEAVkaflkel 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546 108 ---FPAALPAGPDVMVEFFNNGLpiatPTVFLVNVNTIMTFpMFQGAVAADVFMTRLDEV 164
Cdd:COG0526   82 glpYPVLLDPDGELAKAYGVRGI----PTTVLIDKDGKIVA-RHVGPLSPEELEEALEKL 136
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 66-101 7.90e-03

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 34.07  E-value: 7.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 500229546  66 LVLFMQSTCSYCHQFDPVLKQISEQTGIAVFpYSLD 101
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEEYPKVKF-VKVD 48
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-178 3.08e-96

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 276.22  E-value: 3.08e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   1 MNTLRTVVLTSWLLCLSATASTWDDIARLDAAK-------AARQDTSAQTRAADHPPFRLSDGRAVRVENWKLVLFMQST 73
Cdd:PRK13728   1 MSLTKLLLVLLLLMATAVQASTRDEIERLWNPKgmaaqpaQPAADTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546  74 CSYCHQFDPVLKQISEQTGIAVFPYSLDGRGDAAFPAALPAGPDVMVEFFNNgLPIATPTVFLVNVNTIMTFPMFQGAVA 153
Cdd:PRK13728  81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQGATD 159

                        170       180
                 ....*....|....*....|....*
gi 500229546 154 ADVFMTRLDEVFQValsIGGRHATR 178
Cdd:PRK13728 160 AAGFMARMDTVLQM---YGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 4-164 3.64e-51

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.


Pssm-ID: 131785  Cd Length: 153  Bit Score: 161.13  E-value: 3.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546    4 LRTVVLTSWLLCLSATASTWDDIARLDAAKA---ARQDTSAQtraadhppfrlsdGRAVRVENWKLVLFMQSTCSYCHQF 80
Cdd:TIGR02738   2 LRKLLIVLLLLAGLAQASTLDEITNLWAPPQgltAATDNAPQ-------------GRHANQDDYALVFFYQSTCPYCHQF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   81 DPVLKQISEQTGIAVFPYSLDGRGDAAFPAALPAGPDVMVEFFNNGLPIATPTVFLVNVNTIMTFPMFQGAVAADVFMTR 160
Cdd:TIGR02738  69 APVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNPRPVVTPATFLVNVNTRKAYPVLQGAVDEAELANR 148


                  ....
gi 500229546  161 LDEV 164
Cdd:TIGR02738 149 MDEI 152
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 62-161 1.05e-13

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 66.56  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   62 ENWKLVLFMQSTCSYCHQFDPVLKQISEQTGIAVFPYSLDGRGDAAFPAALPagpdvmveffNNGLPIA-----TPTVFL 136
Cdd:pfam13728 129 EEFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYRV----------DNGQAARlgvkrTPALFL 198

                          90       100
                  ....*....|....*....|....*
gi 500229546  137 VNVNTIMTFPMFQGAVAADVFMTRL 161
Cdd:pfam13728 199 VNPPSGDVVPVAAGVLSLDELEERI 223
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 40-164 5.20e-05

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 5.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546  40 SAQTRAADHPPFRLSDGRAVRVENWK----LVLFMQSTCSYCHQFDPVLKQISEQT-GIAVFPYSLDGRGDAA------- 107
Cdd:COG0526    2 KAVGKPAPDFTLTDLDGKPLSLADLKgkpvLVNFWATWCPPCRAEMPVLKELAEEYgGVVFVGVDVDENPEAVkaflkel 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546 108 ---FPAALPAGPDVMVEFFNNGLpiatPTVFLVNVNTIMTFpMFQGAVAADVFMTRLDEV 164
Cdd:COG0526   82 glpYPVLLDPDGELAKAYGVRGI----PTTVLIDKDGKIVA-RHVGPLSPEELEEALEKL 136
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
64-157 1.04e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.02  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500229546   64 WKLVLFMQSTCSYCHQFDPVLKQISEQTGI---AVFPYSLDGRGdAAFPAALPAGPDVMVEFFNNgLPI-ATPTVFLVNV 139
Cdd:pfam13098   6 PVLVVFTDPDCPYCKKLKKELLEDPDVTVYlgpNFVFIAVNIWC-AKEVAKAFTDILENKELGRK-YGVrGTPTIVFFDG 83

                          90
                  ....*....|....*...
gi 500229546  140 NTIMTfpMFQGAVAADVF 157
Cdd:pfam13098  84 KGELL--RLPGYVPAEEF 99
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 66-101 7.90e-03

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 34.07  E-value: 7.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 500229546  66 LVLFMQSTCSYCHQFDPVLKQISEQTGIAVFpYSLD 101
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEEYPKVKF-VKVD 48
 
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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