NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446829237|ref|WP_000906493|]
View 

MULTISPECIES: type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB [Escherichia]

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 ...
 6-192 1.85e-74

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: 222.29  E-value: 1.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237   6 LRTAILMAAML-SGCLQAGTLDDIRALEAGKnGRSAPALDGVrlpesnTPPSPgLSEKTSPVWYPLSDGRRVDLQDWKLV 84
Cdd:PRK13728   3 LTKLLLVLLLLmATAVQASTRDEIERLWNPK-GMAAQPAQPA------ADTSA-RTEKPAPRWFRLSNGRQVNLADWKVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  85 LFMQSTCQYCRQFAPVLKSLSQQSGLSVFPVSLDGKGDAEFPDVLPATPDVMVEFFqSGVPVATPTTFLTNVNTMETWPL 164
Cdd:PRK13728  75 LFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFF-PNIPVATPTTFLVNVNTLEALPL 153

                        170       180
                 ....*....|....*....|....*...
gi 446829237 165 LQGAAEAGEVRKRLDDVFRMALDRQAGK 192
Cdd:PRK13728 154 LQGATDAAGFMARMDTVLQMYGGKKGAK 181
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 6-192 1.85e-74

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 222.29  E-value: 1.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237   6 LRTAILMAAML-SGCLQAGTLDDIRALEAGKnGRSAPALDGVrlpesnTPPSPgLSEKTSPVWYPLSDGRRVDLQDWKLV 84
Cdd:PRK13728   3 LTKLLLVLLLLmATAVQASTRDEIERLWNPK-GMAAQPAQPA------ADTSA-RTEKPAPRWFRLSNGRQVNLADWKVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  85 LFMQSTCQYCRQFAPVLKSLSQQSGLSVFPVSLDGKGDAEFPDVLPATPDVMVEFFqSGVPVATPTTFLTNVNTMETWPL 164
Cdd:PRK13728  75 LFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFF-PNIPVATPTTFLVNVNTLEALPL 153

                        170       180
                 ....*....|....*....|....*...
gi 446829237 165 LQGAAEAGEVRKRLDDVFRMALDRQAGK 192
Cdd:PRK13728 154 LQGATDAAGFMARMDTVLQMYGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 6-181 8.51e-62

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: 189.24  E-value: 8.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237    6 LRTAILMAAMLSGCLQAGTLDDIRALEAGkngrsapaldgvrlpesntPPSPGLSEKTSPVwyplsdGRRVDLQDWKLVL 85
Cdd:TIGR02738   2 LRKLLIVLLLLAGLAQASTLDEITNLWAP-------------------PQGLTAATDNAPQ------GRHANQDDYALVF 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237   86 FMQSTCQYCRQFAPVLKSLSQQSGLSVFPVSLDGKGDAEFPDVLPATPDVMVEFFQSGVPVATPTTFLTNVNTMETWPLL 165
Cdd:TIGR02738  57 FYQSTCPYCHQFAPVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNPRPVVTPATFLVNVNTRKAYPVL 136

                         170
                  ....*....|....*.
gi 446829237  166 QGAAEAGEVRKRLDDV 181
Cdd:TIGR02738 137 QGAVDEAELANRMDEI 152
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 79-178 5.52e-14

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: 67.72  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237   79 QDWKLVLFMQSTCQYCRQFAPVLKSLSQQSGLSVFPVSLDGKGDAEFPDVLPATPdvmvEFFQSGVPVaTPTTFLTNVNT 158
Cdd:pfam13728 129 EEFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYRVDNG----QAARLGVKR-TPALFLVNPPS 203

                          90       100
                  ....*....|....*....|
gi 446829237  159 METWPLLQGAAEAGEVRKRL 178
Cdd:pfam13728 204 GDVVPVAAGVLSLDELEERI 223
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 69-181 1.75e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 48.53  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  69 PLSDGRRVDLQDWK----LVLFMQSTCQYCRQFAPVLKSLSQQ-SGLSVFPVSLDGKGDA----------EFPDVLPATP 133
Cdd:COG0526   14 TDLDGKPLSLADLKgkpvLVNFWATWCPPCRAEMPVLKELAEEyGGVVFVGVDVDENPEAvkaflkelglPYPVLLDPDG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446829237 134 DVMVEFfqsGVPvATPTTFLTNVNTMETWPLLqGAAEAGEVRKRLDDV 181
Cdd:COG0526   94 ELAKAY---GVR-GIPTTVLIDKDGKIVARHV-GPLSPEELEEALEKL 136
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 69-153 1.13e-05

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 42.99  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  69 PLSDGRRVDLQDWK----LVLFMQSTCQYCRQFAPVLKSLSQQ---SGLSVFPVSLDGKGDAE-----------FPDVLP 130
Cdd:cd02966    5 PDLDGKPVSLSDLKgkvvLVNFWASWCPPCRAEMPELEALAKEykdDGVEVVGVNVDDDDPAAvkaflkkygitFPVLLD 84

                         90       100
                 ....*....|....*....|...
gi 446829237 131 ATPDVMVEFfqsGVpVATPTTFL 153
Cdd:cd02966   85 PDGELAKAY---GV-RGLPTTFL 103
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 6-192 1.85e-74

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 222.29  E-value: 1.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237   6 LRTAILMAAML-SGCLQAGTLDDIRALEAGKnGRSAPALDGVrlpesnTPPSPgLSEKTSPVWYPLSDGRRVDLQDWKLV 84
Cdd:PRK13728   3 LTKLLLVLLLLmATAVQASTRDEIERLWNPK-GMAAQPAQPA------ADTSA-RTEKPAPRWFRLSNGRQVNLADWKVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  85 LFMQSTCQYCRQFAPVLKSLSQQSGLSVFPVSLDGKGDAEFPDVLPATPDVMVEFFqSGVPVATPTTFLTNVNTMETWPL 164
Cdd:PRK13728  75 LFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFF-PNIPVATPTTFLVNVNTLEALPL 153

                        170       180
                 ....*....|....*....|....*...
gi 446829237 165 LQGAAEAGEVRKRLDDVFRMALDRQAGK 192
Cdd:PRK13728 154 LQGATDAAGFMARMDTVLQMYGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 6-181 8.51e-62

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: 189.24  E-value: 8.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237    6 LRTAILMAAMLSGCLQAGTLDDIRALEAGkngrsapaldgvrlpesntPPSPGLSEKTSPVwyplsdGRRVDLQDWKLVL 85
Cdd:TIGR02738   2 LRKLLIVLLLLAGLAQASTLDEITNLWAP-------------------PQGLTAATDNAPQ------GRHANQDDYALVF 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237   86 FMQSTCQYCRQFAPVLKSLSQQSGLSVFPVSLDGKGDAEFPDVLPATPDVMVEFFQSGVPVATPTTFLTNVNTMETWPLL 165
Cdd:TIGR02738  57 FYQSTCPYCHQFAPVLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNPRPVVTPATFLVNVNTRKAYPVL 136

                         170
                  ....*....|....*.
gi 446829237  166 QGAAEAGEVRKRLDDV 181
Cdd:TIGR02738 137 QGAVDEAELANRMDEI 152
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 79-178 5.52e-14

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: 67.72  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237   79 QDWKLVLFMQSTCQYCRQFAPVLKSLSQQSGLSVFPVSLDGKGDAEFPDVLPATPdvmvEFFQSGVPVaTPTTFLTNVNT 158
Cdd:pfam13728 129 EEFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNYRVDNG----QAARLGVKR-TPALFLVNPPS 203

                          90       100
                  ....*....|....*....|
gi 446829237  159 METWPLLQGAAEAGEVRKRL 178
Cdd:pfam13728 204 GDVVPVAAGVLSLDELEERI 223
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 69-181 1.75e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 48.53  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  69 PLSDGRRVDLQDWK----LVLFMQSTCQYCRQFAPVLKSLSQQ-SGLSVFPVSLDGKGDA----------EFPDVLPATP 133
Cdd:COG0526   14 TDLDGKPLSLADLKgkpvLVNFWATWCPPCRAEMPVLKELAEEyGGVVFVGVDVDENPEAvkaflkelglPYPVLLDPDG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446829237 134 DVMVEFfqsGVPvATPTTFLTNVNTMETWPLLqGAAEAGEVRKRLDDV 181
Cdd:COG0526   94 ELAKAY---GVR-GIPTTVLIDKDGKIVARHV-GPLSPEELEEALEKL 136
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 69-153 1.13e-05

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 42.99  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  69 PLSDGRRVDLQDWK----LVLFMQSTCQYCRQFAPVLKSLSQQ---SGLSVFPVSLDGKGDAE-----------FPDVLP 130
Cdd:cd02966    5 PDLDGKPVSLSDLKgkvvLVNFWASWCPPCRAEMPELEALAKEykdDGVEVVGVNVDDDDPAAvkaflkkygitFPVLLD 84

                         90       100
                 ....*....|....*....|...
gi 446829237 131 ATPDVMVEFfqsGVpVATPTTFL 153
Cdd:cd02966   85 PDGELAKAY---GV-RGLPTTFL 103
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-153 2.61e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446829237  69 PLSDGRRVDLQDWK----LVLFMQSTCQYCRQFAPVLKSLSQQ---SGLSVFPVSLDG---------KGDAEFPDVLPAT 132
Cdd:COG1225    7 PDLDGKTVSLSDLRgkpvVLYFYATWCPGCTAELPELRDLYEEfkdKGVEVLGVSSDSdeahkkfaeKYGLPFPLLSDPD 86

                         90       100
                 ....*....|....*....|.
gi 446829237 133 PDVMVEFfqsGVPvATPTTFL 153
Cdd:COG1225   87 GEVAKAY---GVR-GTPTTFL 103
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 83-148 9.37e-04

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: 37.15  E-value: 9.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446829237  83 LVLFMQSTCQYCRQFAPVLKSLSQQSGLSVFpVSLDgkgDAEFPDV-----LPATPDVMveFFQSGVPVAT 148
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEEYPKVKF-VKVD---VDENPELaeeygVRSIPTFL--FFKNGKEVDR 78
 
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