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Conserved domains on  [gi|738619055|ref|WP_036528767|]
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conjugal transfer protein TraF [Novosphingobium resinovorum]

Protein Classification

conjugal transfer protein TraF( domain architecture ID 10617434)

conjugal transfer protein TraF is involved in the conjugative transfer of plasmid DNA and may catalyze the reduction or isomerization 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
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 47-260 5.66e-102

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: 296.53  E-value: 5.66e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   47 GQWFYCSKPKPRETRPASPQAPEP------------SAAERMAAIAKELDELKARAILDPSEENVIAYVRFQREQLDRAS 114
Cdd:pfam13728   1 GWFWYEDPPKPPEPKPEKPAPPPAakpalkppppeeSATMSPAWLRKELEELRDQAILNPTEENVKAYLRLQRIARDKAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  115 TFADTWQRALWQHPDIDYTLQRPVSTVGKRAWLDNRKADRDAVLTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRM 194
Cdd:pfam13728  81 RFADVWQRVLLTNPELDYTLDRPVSNLARKAYLAQRKEEREAALKSLAEEFGLIFFYRGDCPYCEAQAPILQAFADKYGW 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738619055  195 AVMAVSMDGGPNKEFPNYVVDTGQRARMGLTgnETPALVLFDTQTKRTIPVGYGILSADEIMDRIF 260
Cdd:pfam13728 161 TVRPVSVDGRPLPGFPNYRVDNGQAARLGVK--RTPALFLVNPPSGDVVPVAAGVLSLDELEERIL 224
 
Name Accession Description Interval E-value
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 47-260 5.66e-102

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: 296.53  E-value: 5.66e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   47 GQWFYCSKPKPRETRPASPQAPEP------------SAAERMAAIAKELDELKARAILDPSEENVIAYVRFQREQLDRAS 114
Cdd:pfam13728   1 GWFWYEDPPKPPEPKPEKPAPPPAakpalkppppeeSATMSPAWLRKELEELRDQAILNPTEENVKAYLRLQRIARDKAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  115 TFADTWQRALWQHPDIDYTLQRPVSTVGKRAWLDNRKADRDAVLTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRM 194
Cdd:pfam13728  81 RFADVWQRVLLTNPELDYTLDRPVSNLARKAYLAQRKEEREAALKSLAEEFGLIFFYRGDCPYCEAQAPILQAFADKYGW 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738619055  195 AVMAVSMDGGPNKEFPNYVVDTGQRARMGLTgnETPALVLFDTQTKRTIPVGYGILSADEIMDRIF 260
Cdd:pfam13728 161 TVRPVSVDGRPLPGFPNYRVDNGQAARLGVK--RTPALFLVNPPSGDVVPVAAGVLSLDELEERIL 224
TraF-like TIGR02740
TraF-like protein; This protein is related to the F-type conjugation system pilus assembly ...
 12-271 5.95e-92

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: 272.75  E-value: 5.95e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   12 LALMPMTV------NAQEAGASRDTIDGQSPDDFYCGERRLGQWFYCSKPK--PRETRPASPQAP-EPSAAERMAAIAKE 82
Cdd:TIGR02740   1 LPLLALAVvvilslAASAAHAQESDTPFVSGQAFYKDEKRGWFWYEDPPPKeeEEPLEPAPPAPPaQQPAREELAPFSVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   83 -----LDELKARAILDPSEENVIAYVRFQREQLDRASTFADTWQRALWQHPDIDYTLQRPVSTVGKRAWLDNRKADRDAV 157
Cdd:TIGR02740  81 wlrenLPELRDKAIDNPTPENVRAYLEAQRIMLDKASRFADVSQRVIWTDPILDETLRRPVSTLALDAHDTTAKKQKDRV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  158 LTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRMAVMAVSMDGGPNKEFPNYVVDTGQRARMGLTgnETPALVLFDT 237
Cdd:TIGR02740 161 MKDLAKKSGLFFFFKSDCPYCHQQAPILQAFEDRYGIEVLPVSVDGGPLPGFPNARPDAGQAQQLKIR--TVPAVFLADP 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 738619055  238 QTKRTIPVGYGILSADEIMDRIFMLTNtKVGSDY 271
Cdd:TIGR02740 239 DPNQFTPIGFGVMSADELVDRILLAAH-PAGLIS 271
PRK13703 PRK13703
conjugal pilus assembly protein TraF; Provisional
 48-259 6.11e-40

conjugal pilus assembly protein TraF; Provisional


Pssm-ID: 184259  Cd Length: 248  Bit Score: 138.71  E-value: 6.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  48 QWFYCSKPKPRETRPASPQAP--EPSAAERMAAIAKELDELKARAILDPSEENVIAYVRFQREQLDRASTFADTWQRALW 125
Cdd:PRK13703  26 QWYNEKKNPKEKENKPVPAAPrqEPDIMEKLAVLQTATKRALYEAILYPGVENFVKYFRLQNYWTQQAGLFSMSAKKAML 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 126 QHPDIDYTLQRPVSTVGKRAWLDNRKADRDAVLTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRMAVMAVSMDGGP 205
Cdd:PRK13703 106 AHPELDYNLQYSHYNGTVRNQLAADQAQQRQAIAKLAEHYGLMFFYRGQDPIDGQLAQVINDFRDTYGLSVIPVSVDGVI 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738619055 206 NKEFPNYVVDTGQRARMGLTgnETPALVLFDTQTKRTIPVGYGILSADEIMDRI 259
Cdd:PRK13703 186 NPLLPDSRTDQGQAQRLGVK--YFPALMLVDPKSGSVRPLSYGFITQDDLAKRF 237
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 158-260 3.52e-07

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 48.06  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 158 LTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHrmAVMAVSMDGGPNKE-----------FPNYVVDTGQ-RARMGLT 225
Cdd:cd03011   15 LESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADY--PVVSVALRSGDDGAvarfmqkkgygFPVINDPDGViSARWGVS 92

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 738619055 226 GneTPALVLFDTQTKRTIPVgyGILSADEIMDRIF 260
Cdd:cd03011   93 V--TPAIVIVDPGGIVFVTT--GVTSEWGLRLRLW 123
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 158-259 1.67e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.53  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 158 LTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHR-MAVMAVSMDGGPNK----------EFPNYVVDTGQRAR-MGLT 225
Cdd:COG0526   23 LADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGgVVFVGVDVDENPEAvkaflkelglPYPVLLDPDGELAKaYGVR 102

                         90       100       110
                 ....*....|....*....|....*....|....
gi 738619055 226 GneTPALVLFDTQtKRTIPVGYGILSADEIMDRI 259
Cdd:COG0526  103 G--IPTTVLIDKD-GKIVARHVGPLSPEELEEAL 133
 
Name Accession Description Interval E-value
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 47-260 5.66e-102

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: 296.53  E-value: 5.66e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   47 GQWFYCSKPKPRETRPASPQAPEP------------SAAERMAAIAKELDELKARAILDPSEENVIAYVRFQREQLDRAS 114
Cdd:pfam13728   1 GWFWYEDPPKPPEPKPEKPAPPPAakpalkppppeeSATMSPAWLRKELEELRDQAILNPTEENVKAYLRLQRIARDKAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  115 TFADTWQRALWQHPDIDYTLQRPVSTVGKRAWLDNRKADRDAVLTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRM 194
Cdd:pfam13728  81 RFADVWQRVLLTNPELDYTLDRPVSNLARKAYLAQRKEEREAALKSLAEEFGLIFFYRGDCPYCEAQAPILQAFADKYGW 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738619055  195 AVMAVSMDGGPNKEFPNYVVDTGQRARMGLTgnETPALVLFDTQTKRTIPVGYGILSADEIMDRIF 260
Cdd:pfam13728 161 TVRPVSVDGRPLPGFPNYRVDNGQAARLGVK--RTPALFLVNPPSGDVVPVAAGVLSLDELEERIL 224
TraF-like TIGR02740
TraF-like protein; This protein is related to the F-type conjugation system pilus assembly ...
 12-271 5.95e-92

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: 272.75  E-value: 5.95e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   12 LALMPMTV------NAQEAGASRDTIDGQSPDDFYCGERRLGQWFYCSKPK--PRETRPASPQAP-EPSAAERMAAIAKE 82
Cdd:TIGR02740   1 LPLLALAVvvilslAASAAHAQESDTPFVSGQAFYKDEKRGWFWYEDPPPKeeEEPLEPAPPAPPaQQPAREELAPFSVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   83 -----LDELKARAILDPSEENVIAYVRFQREQLDRASTFADTWQRALWQHPDIDYTLQRPVSTVGKRAWLDNRKADRDAV 157
Cdd:TIGR02740  81 wlrenLPELRDKAIDNPTPENVRAYLEAQRIMLDKASRFADVSQRVIWTDPILDETLRRPVSTLALDAHDTTAKKQKDRV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  158 LTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRMAVMAVSMDGGPNKEFPNYVVDTGQRARMGLTgnETPALVLFDT 237
Cdd:TIGR02740 161 MKDLAKKSGLFFFFKSDCPYCHQQAPILQAFEDRYGIEVLPVSVDGGPLPGFPNARPDAGQAQQLKIR--TVPAVFLADP 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 738619055  238 QTKRTIPVGYGILSADEIMDRIFMLTNtKVGSDY 271
Cdd:TIGR02740 239 DPNQFTPIGFGVMSADELVDRILLAAH-PAGLIS 271
TraF TIGR02739
type-F conjugative transfer system pilin assembly protein TraF; This protein is part of a ...
 54-271 2.69e-57

type-F conjugative transfer system pilin assembly protein TraF; 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 and has been shown to be localized to the periplasm. Unlike the related protein TrbB (TIGR02738), TraF does not contain a conserved pair of cysteines and has been shown not to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. Even more closely related than TrbB is a clade of genes (TIGR02740) which do contain the CXXC motif, but it is unclear whether these genes are involved in type-F conjugation systems per se.


Pssm-ID: 274274  Cd Length: 256  Bit Score: 183.75  E-value: 2.69e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055   54 KPKPRETRPASPQApepSAAERMAAIAKELDELKARAILDPSEENVIAYVRFQREQLDRASTFADTWQRALWQHPDIDYT 133
Cdd:TIGR02739  44 KPVPLQPSQEPPPL---SPTEQMKLLRQETKEALNQAILNPSVENFARYMRLQRFWTKQSSQFSMTWQKALLAHPELDYT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  134 LQRPVSTVGKRAWLDNRKADRDAVLTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRMAVMAVSMDGGPNKEFPNYV 213
Cdd:TIGR02739 121 LTHPTSNAARQVYLQLEKEQKEKAIQQLSQSYGLFFFYRGKSPISQKMAPVIQAFAKEYGISVIPISVDGTLIPGLPNSR 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 738619055  214 VDTGQRARMGLTgnETPALVLFDTQTKRTIPVGYGILSADEIMDRIFMLTNTKVGSDY 271
Cdd:TIGR02739 201 SDSGQAQHLGVK--YFPALYLVNPKSQKMSPLAYGFISQDELKERILNVLTQFKRPDY 256
PRK13703 PRK13703
conjugal pilus assembly protein TraF; Provisional
 48-259 6.11e-40

conjugal pilus assembly protein TraF; Provisional


Pssm-ID: 184259  Cd Length: 248  Bit Score: 138.71  E-value: 6.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  48 QWFYCSKPKPRETRPASPQAP--EPSAAERMAAIAKELDELKARAILDPSEENVIAYVRFQREQLDRASTFADTWQRALW 125
Cdd:PRK13703  26 QWYNEKKNPKEKENKPVPAAPrqEPDIMEKLAVLQTATKRALYEAILYPGVENFVKYFRLQNYWTQQAGLFSMSAKKAML 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 126 QHPDIDYTLQRPVSTVGKRAWLDNRKADRDAVLTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHRMAVMAVSMDGGP 205
Cdd:PRK13703 106 AHPELDYNLQYSHYNGTVRNQLAADQAQQRQAIAKLAEHYGLMFFYRGQDPIDGQLAQVINDFRDTYGLSVIPVSVDGVI 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738619055 206 NKEFPNYVVDTGQRARMGLTgnETPALVLFDTQTKRTIPVGYGILSADEIMDRI 259
Cdd:PRK13703 186 NPLLPDSRTDQGQAQRLGVK--YFPALMLVDPKSGSVRPLSYGFITQDDLAKRF 237
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 120-259 2.92e-14

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: 68.29  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  120 WQRALWQHPDIDYTLQrpvstvgkrawlDNRKADRDAvltsLSQRYGLFYFYAQSCGACELFAPILRSVADSHRMAVMAV 199
Cdd:TIGR02738  23 EITNLWAPPQGLTAAT------------DNAPQGRHA----NQDDYALVFFYQSTCPYCHQFAPVLKRFSQQFGLPVYAF 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738619055  200 SMDGGPNKEFPNYVVDTGQRARMGLTGNE---TPALVLFDTQTKRTIPVGYGILSADEIMDRI 259
Cdd:TIGR02738  87 SLDGQGLTGFPDPLPATPEVMQTFFPNPRpvvTPATFLVNVNTRKAYPVLQGAVDEAELANRM 149
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 165-270 3.18e-07

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 49.34  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 165 YGLFYFYAQSCGACELFAPILRSVADSHRMAVMAVSMDGGPNKEFPNyVVDTGQRARMGLTGN---ETPALVLFDTQTKR 241
Cdd:PRK13728  71 WKVVLFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPE-ALPAPPDVMQTFFPNipvATPTTFLVNVNTLE 149

                         90       100       110
                 ....*....|....*....|....*....|..
gi 738619055 242 TIPVGYGILSADEIMDR---IFMLTNTKVGSD 270
Cdd:PRK13728 150 ALPLLQGATDAAGFMARmdtVLQMYGGKKGAK 181
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 158-260 3.52e-07

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 48.06  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 158 LTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHrmAVMAVSMDGGPNKE-----------FPNYVVDTGQ-RARMGLT 225
Cdd:cd03011   15 LESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADY--PVVSVALRSGDDGAvarfmqkkgygFPVINDPDGViSARWGVS 92

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 738619055 226 GneTPALVLFDTQTKRTIPVgyGILSADEIMDRIF 260
Cdd:cd03011   93 V--TPAIVIVDPGGIVFVTT--GVTSEWGLRLRLW 123
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 158-259 1.67e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.53  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 158 LTSLSQRYGLFYFYAQSCGACELFAPILRSVADSHR-MAVMAVSMDGGPNK----------EFPNYVVDTGQRAR-MGLT 225
Cdd:COG0526   23 LADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGgVVFVGVDVDENPEAvkaflkelglPYPVLLDPDGELAKaYGVR 102

                         90       100       110
                 ....*....|....*....|....*....|....
gi 738619055 226 GneTPALVLFDTQtKRTIPVGYGILSADEIMDRI 259
Cdd:COG0526  103 G--IPTTVLIDKD-GKIVARHVGPLSPEELEEAL 133
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 167-259 1.17e-04

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 40.57  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 167 LFYFYAQSCGACELFAPILRSVADSHRMAVMAVSMDggpnkefpnyvVDTGQR--ARMGLTGneTPALVLF------DTQ 238
Cdd:COG3118   22 LVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVD-----------VDENPElaAQFGVRS--IPTLLLFkdgqpvDRF 88

                         90       100
                 ....*....|....*....|.
gi 738619055 239 TkrtipvgyGILSADEIMDRI 259
Cdd:COG3118   89 V--------GALPKEQLREFL 101
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 167-259 1.58e-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: 36.77  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 167 LFYFYAQSCGACELFAPILRSVADSHRMAVMaVSMDGGPNKEFPnyvvdtgqrARMGLTGneTPALVLF-DTQTKRTIpv 245
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEEYPKVKF-VKVDVDENPELA---------EEYGVRS--IPTFLFFkNGKEVDRV-- 79

                         90
                 ....*....|....
gi 738619055 246 gYGILSADEIMDRI 259
Cdd:cd02947   80 -VGADPKEELEEFL 92
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
167-255 2.78e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 36.63  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055  167 LFYFYAQSCGACELFAPILRSVAD------SHRMAVMaVSMDGGPNKEF-PNYVVDTGQRAR-MGLTGneTPALVLFDTQ 238
Cdd:pfam13098   8 LVVFTDPDCPYCKKLKKELLEDPDvtvylgPNFVFIA-VNIWCAKEVAKaFTDILENKELGRkYGVRG--TPTIVFFDGK 84

                          90
                  ....*....|....*..
gi 738619055  239 TKRTIPVGYgiLSADEI 255
Cdd:pfam13098  85 GELLRLPGY--VPAEEF 99
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 160-238 3.03e-03

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: 36.83  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738619055 160 SLSQRYG---LFYFYAQSCGACELFAPILRSVADSHR---MAVMAVSMDGGPNKEFPNY----------VVDTGQRARMG 223
Cdd:cd02966   13 SLSDLKGkvvLVNFWASWCPPCRAEMPELEALAKEYKddgVEVVGVNVDDDDPAAVKAFlkkygitfpvLLDPDGELAKA 92

                         90
                 ....*....|....*
gi 738619055 224 LTGNETPALVLFDTQ 238
Cdd:cd02966   93 YGVRGLPTTFLIDRD 107
trxA PRK09381
thioredoxin TrxA;
170-246 9.28e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 35.04  E-value: 9.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738619055 170 FYAQSCGACELFAPILRSVADSH--RMAVMAVSMDGGPnkefpnyvvdtGQRARMGLTGneTPALVLFDTQTKRTIPVG 246
Cdd:PRK09381  28 FWAEWCGPCKMIAPILDEIADEYqgKLTVAKLNIDQNP-----------GTAPKYGIRG--IPTLLLFKNGEVAATKVG 93
 
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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