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Conserved domains on  [gi|1345423639|ref|WP_104215828|]
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MULTISPECIES: protein disulfide oxidoreductase [Vibrio]

Protein Classification

protein disulfide oxidoreductase( domain architecture ID 10122406)

protein disulfide oxidoreductase catalyzes dithiol oxidation or disulfide reduction of target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 48-171 9.05e-52

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: 161.70  E-value: 9.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  48 PPMVGVSLSGKPIDVIEMSKEePVLVYFWTTWCVACKFVTPVVDWFSSSYPVVGVSLTSGKDERVQRYMNAKGYSYDNIN 127
Cdd:cd03011     1 PLFTATTLDGEQFDLESLSGK-PVLVYFWATWCPVCRFTSPTVNQLAADYPVVSVALRSGDDGAVARFMQKKGYGFPVIN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1345423639 128 DTQGKIARDWGISLTPTLIVINDGKVTSVTSGITTPIGIAARLW 171
Cdd:cd03011    80 DPDGVISARWGVSVTPAIVIVDPGGIVFVTTGVTSEWGLRLRLW 123
 
Name Accession Description Interval E-value
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 48-171 9.05e-52

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: 161.70  E-value: 9.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  48 PPMVGVSLSGKPIDVIEMSKEePVLVYFWTTWCVACKFVTPVVDWFSSSYPVVGVSLTSGKDERVQRYMNAKGYSYDNIN 127
Cdd:cd03011     1 PLFTATTLDGEQFDLESLSGK-PVLVYFWATWCPVCRFTSPTVNQLAADYPVVSVALRSGDDGAVARFMQKKGYGFPVIN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1345423639 128 DTQGKIARDWGISLTPTLIVINDGKVTSVTSGITTPIGIAARLW 171
Cdd:cd03011    80 DPDGVISARWGVSVTPAIVIVDPGGIVFVTTGVTSEWGLRLRLW 123
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 45-170 4.40e-25

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 93.99  E-value: 4.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  45 QNVPPMVGVSLSGKPIDVIEMsKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYP---VVGVSLTSGKdERVQRYMNAKGY 121
Cdd:COG0526     6 KPAPDFTLTDLDGKPLSLADL-KGKPVLVNFWATWCPPCRAEMPVLKELAEEYGgvvFVGVDVDENP-EAVKAFLKELGL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1345423639 122 SYDNINDTQGKIARDWGISLTPTLIVIN-DGKVTSVTSGITTPIGIAARL 170
Cdd:COG0526    84 PYPVLLDPDGELAKAYGVRGIPTTVLIDkDGKIVARHVGPLSPEELEEAL 133
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 69-153 5.38e-10

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 53.47  E-value: 5.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  69 EPVLVYFWTTWCVACKFVTPVVDWFSSSYP------VVGVSLTSGKDE--RVQRYMNAKGYSYDNINDTQGKIARDWGIS 140
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYEKLKkkknveIVFVSLDRDLEEfkDYLKKMPKDWLSVPFDDDERNELKRKYGVN 81

                          90
                  ....*....|....
gi 1345423639 141 LTPTLIVIN-DGKV 153
Cdd:pfam13905  82 AIPTLVLLDpNGEV 95
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 66-153 8.82e-10

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 53.06  E-value: 8.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  66 SKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYPvvgVSLTSGKdervqryMNAkgysydninDTQGKIARDWGISLTPTL 145
Cdd:TIGR01068  12 SSDKPVLVDFWAPWCGPCKMIAPILEELAKEYE---GKVKFVK-------LNV---------DENPDIAAKYGIRSIPTL 72


                  ....*...
gi 1345423639 146 IVINDGKV 153
Cdd:TIGR01068  73 LLFKNGKE 80
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
48-162 8.87e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 43.84  E-value: 8.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  48 PPMVGVSLSGKPIDVIEMsKEEPVLVYFWTTWCVACKFVTPvvdWFSSSYPVV---GV---SLTSGKDE-RVQRYMNAKG 120
Cdd:PRK03147   42 PNFVLTDLEGKKIELKDL-KGKGVFLNFWGTWCKPCEKEMP---YMNELYPKYkekGVeiiAVNVDETElAVKNFVNRYG 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1345423639 121 YSYDNINDTQGKIARDWGISLTPTLIVIN-DGKVTSVTSGITT 162
Cdd:PRK03147  118 LTFPVAIDKGRQVIDAYGVGPLPTTFLIDkDGKVVKVITGEMT 160
 
Name Accession Description Interval E-value
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 48-171 9.05e-52

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: 161.70  E-value: 9.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  48 PPMVGVSLSGKPIDVIEMSKEePVLVYFWTTWCVACKFVTPVVDWFSSSYPVVGVSLTSGKDERVQRYMNAKGYSYDNIN 127
Cdd:cd03011     1 PLFTATTLDGEQFDLESLSGK-PVLVYFWATWCPVCRFTSPTVNQLAADYPVVSVALRSGDDGAVARFMQKKGYGFPVIN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1345423639 128 DTQGKIARDWGISLTPTLIVINDGKVTSVTSGITTPIGIAARLW 171
Cdd:cd03011    80 DPDGVISARWGVSVTPAIVIVDPGGIVFVTTGVTSEWGLRLRLW 123
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 45-170 4.40e-25

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 93.99  E-value: 4.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  45 QNVPPMVGVSLSGKPIDVIEMsKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYP---VVGVSLTSGKdERVQRYMNAKGY 121
Cdd:COG0526     6 KPAPDFTLTDLDGKPLSLADL-KGKPVLVNFWATWCPPCRAEMPVLKELAEEYGgvvFVGVDVDENP-EAVKAFLKELGL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1345423639 122 SYDNINDTQGKIARDWGISLTPTLIVIN-DGKVTSVTSGITTPIGIAARL 170
Cdd:COG0526    84 PYPVLLDPDGELAKAYGVRGIPTTVLIDkDGKIVARHVGPLSPEELEEAL 133
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 49-159 1.70e-24

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: 91.91  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  49 PMVGVSLSGKPIDVIEMsKEEPVLVYFWTTWCVACKFVTPVVDWFSSSY-----PVVGVSLTSGKDERVQRYMNAKGYSY 123
Cdd:cd02966     1 DFSLPDLDGKPVSLSDL-KGKVVLVNFWASWCPPCRAEMPELEALAKEYkddgvEVVGVNVDDDDPAAVKAFLKKYGITF 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1345423639 124 DNINDTQGKIARDWGISLTPTLIVIN-DGKVTSVTSG 159
Cdd:cd02966    80 PVLLDPDGELAKAYGVRGLPTTFLIDrDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
47-153 8.94e-15

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 67.20  E-value: 8.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  47 VPPMVGVSLSGKPIDVIEMsKEEPVLVYFWTTWCVACkfvTPVVDWFSSSYP--------VVGVSLTSgkDERVQRYMNA 118
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDL-RGKPVVLYFYATWCPGC---TAELPELRDLYEefkdkgveVLGVSSDS--DEAHKKFAEK 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1345423639 119 KGYSYDNINDTQGKIARDWGISLTPTLIVIN-DGKV 153
Cdd:COG1225    75 YGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDpDGKI 110
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 65-175 1.11e-13

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: 63.69  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  65 MSKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYpvvgvsltsgkDERVQ-RYMNAkgysydninDTQGKIARDWGISLTP 143
Cdd:COG3118    15 LESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY-----------GGKVKfVKVDV---------DENPELAAQFGVRSIP 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1345423639 144 TLIVINDGKVTSVTSGITTPIGIAArlWLAKY 175
Cdd:COG3118    75 TLLLFKDGQPVDRFVGALPKEQLRE--FLDKV 104
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 64-159 3.95e-13

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: 61.81  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  64 EMSKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYPVVGVsltsgkdervqrymnAKgysydnIN-DTQGKIARDWGISLT 142
Cdd:cd02947     6 LIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKF---------------VK------VDvDENPELAEEYGVRSI 64

                          90
                  ....*....|....*..
gi 1345423639 143 PTLIVINDGKVTSVTSG 159
Cdd:cd02947    65 PTFLFFKNGKEVDRVVG 81
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 69-153 5.38e-10

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 53.47  E-value: 5.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  69 EPVLVYFWTTWCVACKFVTPVVDWFSSSYP------VVGVSLTSGKDE--RVQRYMNAKGYSYDNINDTQGKIARDWGIS 140
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYEKLKkkknveIVFVSLDRDLEEfkDYLKKMPKDWLSVPFDDDERNELKRKYGVN 81

                          90
                  ....*....|....
gi 1345423639 141 LTPTLIVIN-DGKV 153
Cdd:pfam13905  82 AIPTLVLLDpNGEV 95
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 66-153 8.82e-10

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 53.06  E-value: 8.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  66 SKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYPvvgVSLTSGKdervqryMNAkgysydninDTQGKIARDWGISLTPTL 145
Cdd:TIGR01068  12 SSDKPVLVDFWAPWCGPCKMIAPILEELAKEYE---GKVKFVK-------LNV---------DENPDIAAKYGIRSIPTL 72


                  ....*...
gi 1345423639 146 IVINDGKV 153
Cdd:TIGR01068  73 LLFKNGKE 80
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 47-153 2.56e-07

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 47.19  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  47 VPPMVGVSLSG--KPIDVIEMsKEEPVLVYFWTTWCVACKFVTPVVDWFSS--SYPVVGVSLtsgKDER--VQRYMNAKG 120
Cdd:cd03010     3 APAFSLPALPGpdKTLTSADL-KGKPYLLNVWASWCAPCREEHPVLMALARqgRVPIYGINY---KDNPenALAWLARHG 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1345423639 121 YSYD-NINDTQGKIARDWGISLTPTLIVIN-DGKV 153
Cdd:cd03010    79 NPYAaVGFDPDGRVGIDLGVYGVPETFLIDgDGII 113
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 53-174 4.48e-07

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 46.07  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  53 VSLSGKPIDVIEMSKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYPVvgvsltsgkdervqrymNAKGYSYDniNDTQGK 132
Cdd:pfam00085   3 VVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKG-----------------NVVFAKVD--VDENPD 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1345423639 133 IARDWGISLTPTLIVINDGKVTSVTSGITTPIGIAArlWLAK 174
Cdd:pfam00085  64 LASKYGVRGYPTLIFFKNGQPVDDYVGARPKDALAA--FLKA 103
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 61-152 4.78e-07

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 45.73  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  61 DVIEMSKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYPvvgvsltsgkDERVQRYMNAkgysydninDTQGKIARDWGIS 140
Cdd:cd02956     5 QVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQ----------GQFVLAKVNC---------DAQPQIAQQFGVQ 65

                          90
                  ....*....|..
gi 1345423639 141 LTPTLIVINDGK 152
Cdd:cd02956    66 ALPTVYLFAAGQ 77
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 14-163 1.70e-06

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 45.28  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  14 KQKLRSALLYILFALVVVFGVDYWrTKDVPmqnvppmvgvslsgkpiDVIEMSKEE--PVLVYFWTTWCVACK------F 85
Cdd:COG2143     2 KKLLLLLLLLLLLAAAAAAQEISF-LLDLE-----------------EDLALAKAEgkPILLFFESDWCPYCKklhkevF 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  86 VTP-VVDWFSSSYPVVGVSLTSgkDERVQRYmnaKGYSYdnindTQGKIARDWGISLTPTLIVIN-DGKVTSVTSGITTP 163
Cdd:COG2143    64 SDPeVAAYLKENFVVVQLDAEG--DKEVTDF---DGETL-----TEKELARKYGVRGTPTLVFFDaEGKEIARIPGYLKP 133
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 70-154 3.65e-06

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 44.14  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  70 PVLVYFWTT-WCVACKfvTPVVDwFSSSYP--------VVGVSLTSgkDERVQRYMNAKGYSYDNINDTQGKIARDWGIS 140
Cdd:pfam00578  27 WVVLFFYPAdWTPVCT--TELPA-LADLYEefkklgveVLGVSVDS--PESHKAFAEKYGLPFPLLSDPDGEVARAYGVL 101

                          90       100
                  ....*....|....*....|.
gi 1345423639 141 LT------PTLIVIN-DGKVT 154
Cdd:pfam00578 102 NEeeggalRATFVIDpDGKVR 122
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
48-162 8.87e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 43.84  E-value: 8.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  48 PPMVGVSLSGKPIDVIEMsKEEPVLVYFWTTWCVACKFVTPvvdWFSSSYPVV---GV---SLTSGKDE-RVQRYMNAKG 120
Cdd:PRK03147   42 PNFVLTDLEGKKIELKDL-KGKGVFLNFWGTWCKPCEKEMP---YMNELYPKYkekGVeiiAVNVDETElAVKNFVNRYG 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1345423639 121 YSYDNINDTQGKIARDWGISLTPTLIVIN-DGKVTSVTSGITT 162
Cdd:PRK03147  118 LTFPVAIDKGRQVIDAYGVGPLPTTFLIDkDGKVVKVITGEMT 160
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 18-152 4.77e-05

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 41.90  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  18 RSALLYILFALVVVFGVDYWRTKDVPMQNVPPMVGVSLSGKPI-----------------DVIEMSKeePVLVYFWTTWC 80
Cdd:PRK15412    3 RNVLLIPLIIFLAIAAALLWQLARNAEGDDPTNLESALIGKPVpkfrleslenpgqfyqaDVLTQGK--PVLLNVWATWC 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345423639  81 VACKFVTPVVDWFSSS-YPVVGVSLtsgKDERVQ--RYMNAKGYSYD-NINDTQGKIARDWGISLTPTLIVInDGK 152
Cdd:PRK15412   81 PTCRAEHQYLNQLSAQgIRVVGMNY---KDDRQKaiSWLKELGNPYAlSLFDGDGMLGLDLGVYGAPETFLI-DGN 152
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 70-151 2.00e-04

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 38.74  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  70 PVLVYFWTTWCVACK----FV---TPVVDWFSSSYPVVGVSLTSGkDERVQRYMNAkgysydnindtqgkiardWGISLT 142
Cdd:cd02953    13 PVFVDFTADWCVTCKvnekVVfsdPEVQAALKKDVVLLRADWTKN-DPEITALLKR------------------FGVFGP 73


                  ....*....
gi 1345423639 143 PTLIVINDG 151
Cdd:cd02953    74 PTYLFYGPG 82
trxA PRK09381
thioredoxin TrxA;
53-159 2.43e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 38.89  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  53 VSLSGKPIDVIEMSKEEPVLVYFWTTWCVACKFVTPVVdwfsssypvvgvsltsgkDERVQRYMNAKGYSYDNINDTQGK 132
Cdd:PRK09381    6 IHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPIL------------------DEIADEYQGKLTVAKLNIDQNPGT 67

                          90       100
                  ....*....|....*....|....*..
gi 1345423639 133 iARDWGISLTPTLIVINDGKVTSVTSG 159
Cdd:PRK09381   68 -APKYGIRGIPTLLLFKNGEVAATKVG 93
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 71-159 5.34e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 39.83  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639   71 VLVYFWTTWCVACKFVTPVVDWFSSSYP-----VVGVSLTSGKDER--------VQRYmnakGYSYDNINDTQGKIARDW 137
Cdd:PLN02919   423 VILDFWTYCCINCMHVLPDLEFLEKKYKdqpftVVGVHSAKFDNEKdleairnaVLRY----NISHPVVNDGDMYLWREL 498

                           90       100
                   ....*....|....*....|...
gi 1345423639  138 GISLTPTLIVIN-DGKVTSVTSG 159
Cdd:PLN02919   499 GVSSWPTFAVVSpNGKLIAQLSG 521
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
66-152 2.01e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 36.25  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  66 SKEEPVLVYFWTTWCVAC-KF------VTPVVDWFSSSYPVVGVSLTSGKDerVQRYMNAKgysydninDTQGKIARDWG 138
Cdd:pfam13098   2 GNGKPVLVVFTDPDCPYCkKLkkelleDPDVTVYLGPNFVFIAVNIWCAKE--VAKAFTDI--------LENKELGRKYG 71

                          90
                  ....*....|....
gi 1345423639 139 ISLTPTLIVInDGK 152
Cdd:pfam13098  72 VRGTPTIVFF-DGK 84
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 62-163 2.34e-03

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 36.20  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  62 VIEMSKEEPVLVYFWTTWCVACKFVTPVvdWfsssypvvgvsltsgkdERVQRYMNAKGYSYDNIN-DTQGKIARDWGIS 140
Cdd:cd02963    18 IVPKSFKKPYLIKITSDWCFSCIHIEPV--W-----------------KEVIQELEPLGVGIATVNaGHERRLARKLGAH 78

                          90       100
                  ....*....|....*....|...
gi 1345423639 141 LTPTLIVINDGKVTSVTSGITTP 163
Cdd:cd02963    79 SVPAIVGIINGQVTFYHDSSFTK 101
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 56-148 4.09e-03

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 35.74  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  56 SGKPIDvIEMSKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYP-----VVGVSLTSGKDER--------VQRYmnakGYS 122
Cdd:cd03012    12 TDKPLS-LAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKddglvVIGVHSPEFAFERdlanvksaVLRY----GIT 86

                          90       100
                  ....*....|....*....|....*.
gi 1345423639 123 YDNINDTQGKIARDWGISLTPTLIVI 148
Cdd:cd03012    87 YPVANDNDYATWRAYGNQYWPALYLI 112
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 61-162 7.70e-03

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: 35.75  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345423639  61 DVIEMSKEEPVLVYFWTTWCVACKFVTPVVDWFSSSY--PVVGVSLTSGKDERVQRYMNAKGysydnindtqgkIARDWG 138
Cdd:pfam13728 122 AALKSLAEEFGLIFFYRGDCPYCEAQAPILQAFADKYgwTVRPVSVDGRPLPGFPNYRVDNG------------QAARLG 189

                          90       100
                  ....*....|....*....|....*.
gi 1345423639 139 ISLTPTLIVIN--DGKVTSVTSGITT 162
Cdd:pfam13728 190 VKRTPALFLVNppSGDVVPVAAGVLS 215
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 57-98 9.85e-03

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 34.26  E-value: 9.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1345423639  57 GKPIDVIEMSKEEPVLVYFWTTWCVACKFVTPVVDWFSSSYP 98
Cdd:cd02999     7 NIALDLMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFP 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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