NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495600318|ref|WP_008324897|]
View 

MULTISPECIES: F-type conjugal transfer protein TrbB [Enterobacteriaceae]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
4-185 4.10e-80

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member PRK13728:

Pssm-ID: 469754  Cd Length: 181  Bit Score: 236.54  E-value: 4.10e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   4 KFAVSLLLMFPLLAGAGVRDELAALDAAKTN-VPAGVSARPQSAVS---PQSLMALPDGRQANMKDYAVVLFMQAHCQYS 79
Cdd:PRK13728   5 KLLLVLLLLMATAVQASTRDEIERLWNPKGMaAQPAQPAADTSARTekpAPRWFRLSNGRQVNLADWKVVLFMQGHCPYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318  80 AKFDPLVKGWADQHQIKIYPYTLDGGGDTSFPTPLiprktdPASPiaDEIITFFGNgLPIATPTAFMVNVNTLKAYPLTQ 159
Cdd:PRK13728  85 HQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEAL------PAPP--DVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQ 155
                        170       180
                 ....*....|....*....|....*.
gi 495600318 160 GMMDIPALESRMASLIQADLDNVDPK 185
Cdd:PRK13728 156 GATDAAGFMARMDTVLQMYGGKKGAK 181
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
4-185 4.10e-80

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 236.54  E-value: 4.10e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   4 KFAVSLLLMFPLLAGAGVRDELAALDAAKTN-VPAGVSARPQSAVS---PQSLMALPDGRQANMKDYAVVLFMQAHCQYS 79
Cdd:PRK13728   5 KLLLVLLLLMATAVQASTRDEIERLWNPKGMaAQPAQPAADTSARTekpAPRWFRLSNGRQVNLADWKVVLFMQGHCPYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318  80 AKFDPLVKGWADQHQIKIYPYTLDGGGDTSFPTPLiprktdPASPiaDEIITFFGNgLPIATPTAFMVNVNTLKAYPLTQ 159
Cdd:PRK13728  85 HQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEAL------PAPP--DVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQ 155
                        170       180
                 ....*....|....*....|....*.
gi 495600318 160 GMMDIPALESRMASLIQADLDNVDPK 185
Cdd:PRK13728 156 GATDAAGFMARMDTVLQMYGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
9-175 1.55e-40

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: 134.93  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318    9 LLLMFPLLAGAGVRDELAALDAAktnvPAGVSARPQSAvspqslmalPDGRQANMKDYAVVLFMQAHCQYSAKFDPLVKG 88
Cdd:TIGR02738   8 VLLLLAGLAQASTLDEITNLWAP----PQGLTAATDNA---------PQGRHANQDDYALVFFYQSTCPYCHQFAPVLKR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   89 WADQHQIKIYPYTLDGGGDTSFPTPLiprktdPASPiaDEIITFFGNGLPIATPTAFMVNVNTLKAYPLTQGMMDIPALE 168
Cdd:TIGR02738  75 FSQQFGLPVYAFSLDGQGLTGFPDPL------PATP--EVMQTFFPNPRPVVTPATFLVNVNTRKAYPVLQGAVDEAELA 146

                  ....*..
gi 495600318  169 SRMASLI 175
Cdd:TIGR02738 147 NRMDEIL 153
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
64-170 1.25e-08

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: 52.69  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   64 KDYAVVLFMQAHCQYSAKFDPLVKGWADQHQIKIYPYTLDGGGDTSFPTPLiprktdPASPIADEIitffgnGLPIaTPT 143
Cdd:pfam13728 129 EEFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYR------VDNGQAARL------GVKR-TPA 195
                          90       100
                  ....*....|....*....|....*..
gi 495600318  144 AFMVNVNTLKAYPLTQGMMDIPALESR 170
Cdd:pfam13728 196 LFLVNPPSGDVVPVAAGVLSLDELEER 222
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
4-185 4.10e-80

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 236.54  E-value: 4.10e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   4 KFAVSLLLMFPLLAGAGVRDELAALDAAKTN-VPAGVSARPQSAVS---PQSLMALPDGRQANMKDYAVVLFMQAHCQYS 79
Cdd:PRK13728   5 KLLLVLLLLMATAVQASTRDEIERLWNPKGMaAQPAQPAADTSARTekpAPRWFRLSNGRQVNLADWKVVLFMQGHCPYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318  80 AKFDPLVKGWADQHQIKIYPYTLDGGGDTSFPTPLiprktdPASPiaDEIITFFGNgLPIATPTAFMVNVNTLKAYPLTQ 159
Cdd:PRK13728  85 HQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEAL------PAPP--DVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQ 155
                        170       180
                 ....*....|....*....|....*.
gi 495600318 160 GMMDIPALESRMASLIQADLDNVDPK 185
Cdd:PRK13728 156 GATDAAGFMARMDTVLQMYGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
9-175 1.55e-40

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: 134.93  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318    9 LLLMFPLLAGAGVRDELAALDAAktnvPAGVSARPQSAvspqslmalPDGRQANMKDYAVVLFMQAHCQYSAKFDPLVKG 88
Cdd:TIGR02738   8 VLLLLAGLAQASTLDEITNLWAP----PQGLTAATDNA---------PQGRHANQDDYALVFFYQSTCPYCHQFAPVLKR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   89 WADQHQIKIYPYTLDGGGDTSFPTPLiprktdPASPiaDEIITFFGNGLPIATPTAFMVNVNTLKAYPLTQGMMDIPALE 168
Cdd:TIGR02738  75 FSQQFGLPVYAFSLDGQGLTGFPDPL------PATP--EVMQTFFPNPRPVVTPATFLVNVNTRKAYPVLQGAVDEAELA 146

                  ....*..
gi 495600318  169 SRMASLI 175
Cdd:TIGR02738 147 NRMDEIL 153
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
64-170 1.25e-08

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: 52.69  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   64 KDYAVVLFMQAHCQYSAKFDPLVKGWADQHQIKIYPYTLDGGGDTSFPTPLiprktdPASPIADEIitffgnGLPIaTPT 143
Cdd:pfam13728 129 EEFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYR------VDNGQAARL------GVKR-TPA 195
                          90       100
                  ....*....|....*....|....*..
gi 495600318  144 AFMVNVNTLKAYPLTQGMMDIPALESR 170
Cdd:pfam13728 196 LFLVNPPSGDVVPVAAGVLSLDELEER 222
TraF-like TIGR02740
TraF-like protein; This protein is related to the F-type conjugation system pilus assembly ...
64-172 3.88e-06

TraF-like protein; This protein is related to the F-type conjugation system pilus assembly proteins TraF (TIGR02739)and TrbB (TIGR02738) both of which exhibit a thioredoxin fold. The protein represented by this model has the same length and architecture as TraF, but lacks the CXXC-motif found in TrbB and believed to be responsible for the disulfide isomerase activity of that protein.


Pssm-ID: 274275  Cd Length: 271  Bit Score: 45.87  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495600318   64 KDYAVVLFMQAHCQYSAKFDPLVKGWADQHQIKIYPYTLDGGGDTSFPtpliprKTDPASPIADE--IITffgnglpiaT 141
Cdd:TIGR02740 166 KKSGLFFFFKSDCPYCHQQAPILQAFEDRYGIEVLPVSVDGGPLPGFP------NARPDAGQAQQlkIRT---------V 230
                          90       100       110
                  ....*....|....*....|....*....|.
gi 495600318  142 PTAFMVNVNTLKAYPLTQGMMDIPALESRMA 172
Cdd:TIGR02740 231 PAVFLADPDPNQFTPIGFGVMSADELVDRIL 261
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH