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Conserved domains on  [gi|1800617802|ref|WP_160440974|]
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type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB [Glaesserella parasuis]

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

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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 ...
 4-171 1.04e-58

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: 181.46  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802   4 LKHFVAYLVLGVSSVSNAGIIDELAALEAHKFNQSNDNKTTIKNTT-PIPSEKRYITLSNGKRMDISDWQIVHFMSSTCS 82
Cdd:PRK13728    3 LTKLLLVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSArTEKPAPRWFRLSNGRQVNLADWKVVLFMQGHCP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  83 YCRQFNLVLKQISDSTKIPVFVYSFDGNGDSDFPEAFPTNKEVIDTFFAELPQATPTDFLVNINTMVTLPLTQGATSYHA 162
Cdd:PRK13728   83 YCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDAAG 162


                  ....*....
gi 1800617802 163 FLQRLDEVF 171
Cdd:PRK13728  163 FMARMDTVL 171
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 4-171 1.04e-58

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 181.46  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802   4 LKHFVAYLVLGVSSVSNAGIIDELAALEAHKFNQSNDNKTTIKNTT-PIPSEKRYITLSNGKRMDISDWQIVHFMSSTCS 82
Cdd:PRK13728    3 LTKLLLVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSArTEKPAPRWFRLSNGRQVNLADWKVVLFMQGHCP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  83 YCRQFNLVLKQISDSTKIPVFVYSFDGNGDSDFPEAFPTNKEVIDTFFAELPQATPTDFLVNINTMVTLPLTQGATSYHA 162
Cdd:PRK13728   83 YCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDAAG 162


                  ....*....
gi 1800617802 163 FLQRLDEVF 171
Cdd:PRK13728  163 FMARMDTVL 171
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 69-170 9.81e-35

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: 119.52  E-value: 9.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  69 SDWQIVHFMSSTCSYCRQFNLVLKQISDSTKIPVFVYSFDGNGDSDFPEAFPTNKEVIDTFF-AELPQATPTDFLVNINT 147
Cdd:TIGR02738  50 DDYALVFFYQSTCPYCHQFAPVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFpNPRPVVTPATFLVNVNT 129

                          90       100
                  ....*....|....*....|...
gi 1800617802 148 MVTLPLTQGATSYHAFLQRLDEV 170
Cdd:TIGR02738 130 RKAYPVLQGAVDEAELANRMDEI 152
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 70-167 9.99e-07

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: 47.30  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  70 DWQIVHFMSSTCSYCRQFNLVLKQISDSTKIPVFVYSFDGNGDSDFPeafptnKEVIDTFFAEL--PQATPTDFLVNINT 147
Cdd:pfam13728 130 EFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFP------NYRVDNGQAARlgVKRTPALFLVNPPS 203

                          90       100
                  ....*....|....*....|
gi 1800617802 148 MVTLPLTQGATSYHAFLQRL 167
Cdd:pfam13728 204 GDVVPVAAGVLSLDELEERI 223
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 4-171 1.04e-58

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 181.46  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802   4 LKHFVAYLVLGVSSVSNAGIIDELAALEAHKFNQSNDNKTTIKNTT-PIPSEKRYITLSNGKRMDISDWQIVHFMSSTCS 82
Cdd:PRK13728    3 LTKLLLVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSArTEKPAPRWFRLSNGRQVNLADWKVVLFMQGHCP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  83 YCRQFNLVLKQISDSTKIPVFVYSFDGNGDSDFPEAFPTNKEVIDTFFAELPQATPTDFLVNINTMVTLPLTQGATSYHA 162
Cdd:PRK13728   83 YCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDAAG 162


                  ....*....
gi 1800617802 163 FLQRLDEVF 171
Cdd:PRK13728  163 FMARMDTVL 171
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 69-170 9.81e-35

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: 119.52  E-value: 9.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  69 SDWQIVHFMSSTCSYCRQFNLVLKQISDSTKIPVFVYSFDGNGDSDFPEAFPTNKEVIDTFF-AELPQATPTDFLVNINT 147
Cdd:TIGR02738  50 DDYALVFFYQSTCPYCHQFAPVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFpNPRPVVTPATFLVNVNT 129

                          90       100
                  ....*....|....*....|...
gi 1800617802 148 MVTLPLTQGATSYHAFLQRLDEV 170
Cdd:TIGR02738 130 RKAYPVLQGAVDEAELANRMDEI 152
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 70-167 9.99e-07

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: 47.30  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  70 DWQIVHFMSSTCSYCRQFNLVLKQISDSTKIPVFVYSFDGNGDSDFPeafptnKEVIDTFFAEL--PQATPTDFLVNINT 147
Cdd:pfam13728 130 EFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFP------NYRVDNGQAARlgVKRTPALFLVNPPS 203

                          90       100
                  ....*....|....*....|
gi 1800617802 148 MVTLPLTQGATSYHAFLQRL 167
Cdd:pfam13728 204 GDVVPVAAGVLSLDELEERI 223
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
61-167 2.72e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 35.86  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800617802  61 SNGKRmdisdwQIVHFMSSTCSYCRQFNLVLKQISDSTKI--PVFV-YSFDGNGDSDFPEAFPTNKEVIDtFFAELP-QA 136
Cdd:pfam13098   2 GNGKP------VLVVFTDPDCPYCKKLKKELLEDPDVTVYlgPNFVfIAVNIWCAKEVAKAFTDILENKE-LGRKYGvRG 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1800617802 137 TPTDFLVNINTmvTLPLTQGATSYHAFLQRL 167
Cdd:pfam13098  75 TPTIVFFDGKG--ELLRLPGYVPAEEFLALL 103
 
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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