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Conserved domains on  [gi|446651860|ref|WP_000729206|]
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MULTISPECIES: protein disulfide oxidoreductase [Salmonella]

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 ...
 45-163 3.45e-51

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: 159.77  E-value: 3.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  45 TLTGESTTLATLSEeRPVLLYFWASWCGVCRFTTPAVARLAAEgENVMTVALRSGDDAEVARWLARKGVDFPVVNDAKGA 124
Cdd:cd03011    7 TLDGEQFDLESLSG-KPVLVYFWATWCPVCRFTSPTVNQLAAD-YPVVSVALRSGDDGAVARFMQKKGYGFPVINDPDGV 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446651860 125 LSAGWEISVTPTLVVVSQGRVVFTTSGWTSYWGMKLRLW 163
Cdd:cd03011   85 ISARWGVSVTPAIVIVDPGGIVFVTTGVTSEWGLRLRLW 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 ...
 45-163 3.45e-51

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: 159.77  E-value: 3.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  45 TLTGESTTLATLSEeRPVLLYFWASWCGVCRFTTPAVARLAAEgENVMTVALRSGDDAEVARWLARKGVDFPVVNDAKGA 124
Cdd:cd03011    7 TLDGEQFDLESLSG-KPVLVYFWATWCPVCRFTSPTVNQLAAD-YPVVSVALRSGDDGAVARFMQKKGYGFPVINDPDGV 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446651860 125 LSAGWEISVTPTLVVVSQGRVVFTTSGWTSYWGMKLRLW 163
Cdd:cd03011   85 ISARWGVSVTPAIVIVDPGGIVFVTTGVTSEWGLRLRLW 123
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 43-162 6.79e-26

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 95.91  E-value: 6.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLSEeRPVLLYFWASWCGVCRFTTPAVARLAAE--GENVMTVALRSgDDAEVARWLARKGVDFPVVND 120
Cdd:COG0526   13 LTDLDGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEygGVVFVGVDVDE-NPEAVKAFLKELGLPYPVLLD 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446651860 121 AKGALSAGWEISVTPTLVVV-SQGRVVFTTSGWTSYWGMKLRL 162
Cdd:COG0526   91 PDGELAKAYGVRGIPTTVLIdKDGKIVARHVGPLSPEELEEAL 133
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 46-151 1.13e-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: 55.37  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   46 LTGESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEgenvmtvalRSGDdaevarwlarkgVDFPVVN-DAKGA 124
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKE---------YEGK------------VKFVKLNvDENPD 59

                          90       100
                  ....*....|....*....|....*..
gi 446651860  125 LSAGWEISVTPTLVVVSQGRVVFTTSG 151
Cdd:TIGR01068  60 IAAKYGIRSIPTLLLFKNGKEVDRSVG 86
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 54-136 6.03e-10

bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB;


Pssm-ID: 184456 [Multi-domain]  Cd Length: 521  Bit Score: 56.81  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  54 ATLSEERPVLLYFWASWCGVCRFTTPAVARLAAE----GENVMTVA----LRSGDDAEVARWLArkGVDF---PVVNDAK 122
Cdd:PRK14018  51 VYLKKDKPTLIKFWASWCPLCLSELGETEKWAQDakfsSANLITVAspgfLHEKKDGDFQKWYA--GLDYpklPVLTDNG 128

                         90
                 ....*....|....
gi 446651860 123 GALSAGWEISVTPT 136
Cdd:PRK14018 129 GTLAQSLNISVYPS 142
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 48-148 6.56e-10

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 54.68  E-value: 6.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   48 GESTTLATLSEeRPVLLYFWAS-WCGVCRFTTPAVARLAAEG--ENVMTVALRSGDDA-EVARWLARKGVDFPVVNDAKG 123
Cdd:pfam08534  18 GNTVSLSDFKG-KKVVLNFWPGaFCPTCSAEHPYLEKLNELYkeKGVDVVAVNSDNDAfFVKRFWGKEGLPFPFLSDGNA 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446651860  124 ALSA--GWEISVTP--------TLVVVSQGRVVFT 148
Cdd:pfam08534  97 AFTKalGLPIEEDAsaglrsprYAVIDEDGKVVYL 131
 
Name Accession Description Interval E-value
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 45-163 3.45e-51

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: 159.77  E-value: 3.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  45 TLTGESTTLATLSEeRPVLLYFWASWCGVCRFTTPAVARLAAEgENVMTVALRSGDDAEVARWLARKGVDFPVVNDAKGA 124
Cdd:cd03011    7 TLDGEQFDLESLSG-KPVLVYFWATWCPVCRFTSPTVNQLAAD-YPVVSVALRSGDDGAVARFMQKKGYGFPVINDPDGV 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446651860 125 LSAGWEISVTPTLVVVSQGRVVFTTSGWTSYWGMKLRLW 163
Cdd:cd03011   85 ISARWGVSVTPAIVIVDPGGIVFVTTGVTSEWGLRLRLW 123
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 43-151 2.67e-29

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: 103.86  E-value: 2.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLsEERPVLLYFWASWCGVCRFTTPAVARLAAE----GENVMTVALRSGDDAEVARWLARKGVDFPVV 118
Cdd:cd02966    4 LPDLDGKPVSLSDL-KGKVVLVNFWASWCPPCRAEMPELEALAKEykddGVEVVGVNVDDDDPAAVKAFLKKYGITFPVL 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446651860 119 NDAKGALSAGWEISVTPTLVVVS-QGRVVFTTSG 151
Cdd:cd02966   83 LDPDGELAKAYGVRGLPTTFLIDrDGRIRARHVG 116
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 43-162 6.79e-26

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 95.91  E-value: 6.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLSEeRPVLLYFWASWCGVCRFTTPAVARLAAE--GENVMTVALRSgDDAEVARWLARKGVDFPVVND 120
Cdd:COG0526   13 LTDLDGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEygGVVFVGVDVDE-NPEAVKAFLKELGLPYPVLLD 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446651860 121 AKGALSAGWEISVTPTLVVV-SQGRVVFTTSGWTSYWGMKLRL 162
Cdd:COG0526   91 PDGELAKAYGVRGIPTTVLIdKDGKIVARHVGPLSPEELEEAL 133
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
43-151 1.46e-19

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 79.52  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLsEERPVLLYFWASWCGVCRFTTPAVARLAAE--GENVMTVALRSGDDAEVARWLARKGVDFPVVND 120
Cdd:COG1225    6 LPDLDGKTVSLSDL-RGKPVVLYFYATWCPGCTAELPELRDLYEEfkDKGVEVLGVSSDSDEAHKKFAEKYGLPFPLLSD 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446651860 121 AKGALSAGWEISVTPTLVVV-SQGRVVFTTSG 151
Cdd:COG1225   85 PDGEVAKAYGVRGTPTTFLIdPDGKIRYVWVG 116
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 46-166 4.16e-17

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: 72.16  E-value: 4.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  46 LTGESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEgenvmtvalrSGDDAEVARwlarkgvdfpvVN-DAKGA 124
Cdd:COG3118    5 LTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAE----------YGGKVKFVK-----------VDvDENPE 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446651860 125 LSAGWEISVTPTLVVVSQGRVVFTTSGWTSYWgmKLRLWWAK 166
Cdd:COG3118   64 LAAQFGVRSIPTLLLFKDGQPVDRFVGALPKE--QLREFLDK 103
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 54-151 1.89e-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: 62.58  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  54 ATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEGENVMTVALrsgdDAEVARWLARKgvdfpvvndakgalsagWEISV 133
Cdd:cd02947    5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKV----DVDENPELAEE-----------------YGVRS 63

                         90
                 ....*....|....*...
gi 446651860 134 TPTLVVVSQGRVVFTTSG 151
Cdd:cd02947   64 IPTFLFFKNGKEVDRVVG 81
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 46-151 1.13e-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: 55.37  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   46 LTGESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEgenvmtvalRSGDdaevarwlarkgVDFPVVN-DAKGA 124
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKE---------YEGK------------VKFVKLNvDENPD 59

                          90       100
                  ....*....|....*....|....*..
gi 446651860  125 LSAGWEISVTPTLVVVSQGRVVFTTSG 151
Cdd:TIGR01068  60 IAAKYGIRSIPTLLLFKNGKEVDRSVG 86
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 47-151 1.19e-10

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 57.09  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   47 TGESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEGENVMTVALRSGDDAEVaRWLARKGVDFPVV-NDAKGAL 125
Cdd:TIGR00385  51 PGQFYTADVLTQGKPVLLNVWASWCPPCRAEHPYLNELAKQGLPIVGVDYKDDRQNAI-KFLKELGNPYQLSlFDPDGML 129

                          90       100
                  ....*....|....*....|....*..
gi 446651860  126 SAGWEISVTP-TLVVVSQGRVVFTTSG 151
Cdd:TIGR00385 130 GLDLGVYGAPeTFLVDGNGVIRYRHAG 156
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 43-146 1.66e-10

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: 55.66  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLS-EERPVLLYFWASWCGVCRFTTPAVARLAAEGE-NVMTVALRSgDDAEVARWLARKGVDF-PVVN 119
Cdd:cd03010    8 LPALPGPDKTLTSADlKGKPYLLNVWASWCAPCREEHPVLMALARQGRvPIYGINYKD-NPENALAWLARHGNPYaAVGF 86

                         90       100
                 ....*....|....*....|....*...
gi 446651860 120 DAKGALSAGWEISVTP-TLVVVSQGRVV 146
Cdd:cd03010   87 DPDGRVGIDLGVYGVPeTFLIDGDGIIR 114
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 54-136 6.03e-10

bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB;


Pssm-ID: 184456 [Multi-domain]  Cd Length: 521  Bit Score: 56.81  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  54 ATLSEERPVLLYFWASWCGVCRFTTPAVARLAAE----GENVMTVA----LRSGDDAEVARWLArkGVDF---PVVNDAK 122
Cdd:PRK14018  51 VYLKKDKPTLIKFWASWCPLCLSELGETEKWAQDakfsSANLITVAspgfLHEKKDGDFQKWYA--GLDYpklPVLTDNG 128

                         90
                 ....*....|....
gi 446651860 123 GALSAGWEISVTPT 136
Cdd:PRK14018 129 GTLAQSLNISVYPS 142
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 48-148 6.56e-10

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 54.68  E-value: 6.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   48 GESTTLATLSEeRPVLLYFWAS-WCGVCRFTTPAVARLAAEG--ENVMTVALRSGDDA-EVARWLARKGVDFPVVNDAKG 123
Cdd:pfam08534  18 GNTVSLSDFKG-KKVVLNFWPGaFCPTCSAEHPYLEKLNELYkeKGVDVVAVNSDNDAfFVKRFWGKEGLPFPFLSDGNA 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446651860  124 ALSA--GWEISVTP--------TLVVVSQGRVVFT 148
Cdd:pfam08534  97 AFTKalGLPIEEDAsaglrsprYAVIDEDGKVVYL 131
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 60-145 8.15e-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: 53.08  E-value: 8.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   60 RPVLLYFWASWCGVCRFTTPAVARLA---AEGENVMTVALRSGDDAE----VARWLARKGVDFPVVNDAKGALSAGWEIS 132
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYeklKKKKNVEIVFVSLDRDLEefkdYLKKMPKDWLSVPFDDDERNELKRKYGVN 81

                          90
                  ....*....|....
gi 446651860  133 VTPTLVVV-SQGRV 145
Cdd:pfam13905  82 AIPTLVLLdPNGEV 95
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 45-147 1.91e-09

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: 52.61  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   45 TLTGESTTLATLsEERPVLLYFWAS-WCGVCRFTTPAVARLAAE--GENVMTVALRSGDDAEVARWLARKGVDFPVVNDA 121
Cdd:pfam00578  12 DGDGGTVSLSDY-RGKWVVLFFYPAdWTPVCTTELPALADLYEEfkKLGVEVLGVSVDSPESHKAFAEKYGLPFPLLSDP 90

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446651860  122 KGALSAGWEISVTP-------TLVVVSQGRVVF 147
Cdd:pfam00578  91 DGEVARAYGVLNEEeggalraTFVIDPDGKVRY 123
PRK10996 PRK10996
thioredoxin 2; Provisional
 49-146 7.47e-08

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 48.91  E-value: 7.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  49 ESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEgenvmtvalRSGDdaevarwlarkgVDFPVVN-DAKGALSA 127
Cdd:PRK10996  42 GETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAE---------RSGK------------VRFVKVNtEAERELSA 100

                         90
                 ....*....|....*....
gi 446651860 128 GWEISVTPTLVVVSQGRVV 146
Cdd:PRK10996 101 RFRIRSIPTIMIFKNGQVV 119
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 56-151 2.61e-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: 46.46  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   56 LSEERPVLLYFWASWCGVCRFTTPAVARLAAEGENVMTVAlrsgddaevarwlarkGVDfpvvNDAKGALSAGWEISVTP 135
Cdd:pfam00085  15 QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFA----------------KVD----VDENPDLASKYGVRGYP 74

                          90
                  ....*....|....*.
gi 446651860  136 TLVVVSQGRVVFTTSG 151
Cdd:pfam00085  75 TLIFFKNGQPVDDYVG 90
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 60-146 9.70e-07

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 45.68  E-value: 9.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  60 RPVLLYFWASWCGVCRFTTPAVA----RLAAEGENvMTVALRSGDD---------AEVARWLARKGVDFPVVNDakgaLS 126
Cdd:cd02964   18 KTVGLYFSASWCPPCRAFTPKLVefyeKLKEEGKN-FEIVFVSRDRseesfneyfSEMPPWLAVPFEDEELREL----LE 92

                         90       100
                 ....*....|....*....|.
gi 446651860 127 AGWEISVTPTLVVV-SQGRVV 146
Cdd:cd02964   93 KQFKVEGIPTLVVLkPDGDVV 113
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 56-146 3.00e-06

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: 43.41  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  56 LSEERPVLLYFWASWCGVCRFTTPAVARLAAEGEnvmtvalrsgddaevARWLARKgvdfpvVN-DAKGALSAGWEISVT 134
Cdd:cd02956    9 ESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQ---------------GQFVLAK------VNcDAQPQIAQQFGVQAL 67

                         90
                 ....*....|..
gi 446651860 135 PTLVVVSQGRVV 146
Cdd:cd02956   68 PTVYLFAAGQPV 79
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 56-166 1.02e-05

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 43.83  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  56 LSEERPVLLYFWASWCGVCRFTTPAVARLAAEGenVMTVALRSGDDAEVA-RWLARKGVDFPV-VNDAKGALSAGWEISV 133
Cdd:PRK15412  65 LTQGKPVLLNVWATWCPTCRAEHQYLNQLSAQG--IRVVGMNYKDDRQKAiSWLKELGNPYALsLFDGDGMLGLDLGVYG 142

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446651860 134 TP-TLVVVSQGRVVFTTSG--WTSYWGMKLRLWWAK 166
Cdd:PRK15412 143 APeTFLIDGNGIIRYRHAGdlNPRVWESEIKPLWEK 178
PTZ00051 PTZ00051
thioredoxin; Provisional
 43-151 1.48e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 41.79  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEGENVMTVALRSGDDAEVARwlarkgvdfpvvndak 122
Cdd:PTZ00051   2 VHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAE---------------- 65

                         90       100
                 ....*....|....*....|....*....
gi 446651860 123 galsaGWEISVTPTLVVVSQGRVVFTTSG 151
Cdd:PTZ00051  66 -----KENITSMPTFKVFKNGSVVDTLLG 89
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 63-118 2.51e-05

Thioredoxin (TRX) superfamily; 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 TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 40.37  E-value: 2.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446651860  63 LLYFWASWCGVCRFTTPAVARLAAEGENVMTVALRSGDDAEVARWLARKGVD-FPVV 118
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRYGVGgVPTL 57
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 48-151 3.78e-05

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 41.12  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  48 GESTTLATLsEERPVLLYFWASWCGVCRFTTPAVA----RLAAEGENvMTVALRSGDDAEVA--------RWLArkgVDF 115
Cdd:cd03009    8 GGKVPVSSL-EGKTVGLYFSASWCPPCRAFTPKLVefyeKLKESGKN-FEIVFISWDRDEESfndyfskmPWLA---VPF 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446651860 116 pvvNDAKG--ALSAGWEISVTPTLVVV-SQGRVVfTTSG 151
Cdd:cd03009   83 ---SDRERrsRLNRTFKIEGIPTLIILdADGEVV-TTDA 117
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 58-151 1.68e-04

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 39.50  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  58 EERPVLLYFWASWCGVCR------FTTPAVARLAAegENVMTVALRSGDDAEVarwlarkgVDFPVVNDAKGALSAGWEI 131
Cdd:COG2143   39 EGKPILLFFESDWCPYCKklhkevFSDPEVAAYLK--ENFVVVQLDAEGDKEV--------TDFDGETLTEKELARKYGV 108

                         90       100
                 ....*....|....*....|.
gi 446651860 132 SVTPTLVVVS-QGRVVFTTSG 151
Cdd:COG2143  109 RGTPTLVFFDaEGKEIARIPG 129
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 43-84 1.79e-04

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 39.63  E-value: 1.79e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446651860  43 LHTLTGESTTLAT-LSEERPVLLYFWASWCGVCRFTTPAVARL 84
Cdd:cd02950    3 LEQLAASSTPPEVaLSNGKPTLVEFYADWCTVCQEMAPDVAKL 45
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 62-151 1.81e-04

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: 39.21  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  62 VLLYFWASWCGVCRFTTPAVARLAA--EGENVMTVALRSG------DDAEVARWLARKGVDFPVVNDAKGALSAGWEISV 133
Cdd:cd03012   26 VLLDFWTYCCINCLHTLPYLTDLEQkyKDDGLVVIGVHSPefaferDLANVKSAVLRYGITYPVANDNDYATWRAYGNQY 105

                         90
                 ....*....|....*....
gi 446651860 134 TPTLVVVS-QGRVVFTTSG 151
Cdd:cd03012  106 WPALYLIDpTGNVRHVHFG 124
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 56-113 1.96e-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: 1.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446651860  56 LSEERPVLLYFWASWCGVCR------FTTPAVArlAAEGENVmtVALR---SGDDAEVARWLARKGV 113
Cdd:cd02953    8 LAQGKPVFVDFTADWCVTCKvnekvvFSDPEVQ--AALKKDV--VLLRadwTKNDPEITALLKRFGV 70
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
43-146 2.04e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 39.99  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLsEERPVLLYFWASWCGVCRFTTPAVARLAAE--GENVMTVALRSGD-DAEVARWLARKGVDFPVVN 119
Cdd:PRK03147  46 LTDLEGKKIELKDL-KGKGVFLNFWGTWCKPCEKEMPYMNELYPKykEKGVEIIAVNVDEtELAVKNFVNRYGLTFPVAI 124

                         90       100
                 ....*....|....*....|....*...
gi 446651860 120 DAKGALSAGWEISVTPTLVVVSQ-GRVV 146
Cdd:PRK03147 125 DKGRQVIDAYGVGPLPTTFLIDKdGKVV 152
trxA PRK09381
thioredoxin TrxA;
46-95 2.23e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 38.89  E-value: 2.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446651860  46 LTGESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEGENVMTVA 95
Cdd:PRK09381   8 LTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVA 57
mauD cd02967
Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD ...
 43-146 2.74e-04

Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD gene found in methylotrophic bacteria, which are able to use methylamine as a sole carbon source and a nitrogen source. mauD is an essential accessory protein for the biosynthesis of methylamine dehydrogenase (MADH), the enzyme that catalyzes the oxidation of methylamine and other primary amines. MADH possesses an alpha2beta2 subunit structure; the alpha subunit is also referred to as the large subunit. Each beta (small) subunit contains a tryptophan tryptophylquinone (TTQ) prosthetic group. Accessory proteins are essential for the proper transport of MADH to the periplasm, TTQ synthesis and the formation of several structural disulfide bonds. Bacterial mutants containing an insertion on the mauD gene were unable to grow on methylamine as a sole carbon source, were found to lack the MADH small subunit and had decreased amounts of the MADH large subunit.


Pssm-ID: 239265  Cd Length: 114  Bit Score: 38.54  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAEGENVMTVALRS-GDDAEVARWLARKGVD-FPVVND 120
Cdd:cd02967    5 LTTIDGAPVRIGGISPGRPTLLFFLSPTCPVCKKLLPVIRSIARAEADWLDVVLASdGEKAEHQRFLKKHGLEaFPYVLS 84

                         90       100
                 ....*....|....*....|....*..
gi 446651860 121 AkgALSAGWEISVTPTLVVV-SQGRVV 146
Cdd:cd02967   85 A--ELGMAYQVSKLPYAVLLdEAGVIA 109
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 49-151 8.94e-04

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 36.87  E-value: 8.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  49 ESTTLATLSEERPVLLYFWASWCGVCRFTTPAVARLAAE-GENVMTVALrsgdDAEvarwlarkgvDFPVVndakgalSA 127
Cdd:cd02984    4 EFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSI----EAE----------ELPEI-------SE 62

                         90       100
                 ....*....|....*....|....
gi 446651860 128 GWEISVTPTLVVVSQGRVVFTTSG 151
Cdd:cd02984   63 KFEITAVPTFVFFRNGTIVDRVSG 86
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 43-87 1.14e-03

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 36.53  E-value: 1.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446651860  43 LHtLTGESTTlATLSEERPVLLYFWASWCGVCRFTTPAVARlAAE 87
Cdd:cd02997    3 VH-LTDEDFR-KFLKKEKHVLVMFYAPWCGHCKKMKPEFTK-AAT 44
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
57-142 2.25e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 35.86  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   57 SEERPVLLYFWASWCGVCRfttpavaRLAAEGENVMTVALRSGDDAE---VARWLARKGVDFPVVNDAKGALSAGWEISV 133
Cdd:pfam13098   2 GNGKPVLVVFTDPDCPYCK-------KLKKELLEDPDVTVYLGPNFVfiaVNIWCAKEVAKAFTDILENKELGRKYGVRG 74


                  ....*....
gi 446651860  134 TPTLVVVSQ 142
Cdd:pfam13098  75 TPTIVFFDG 83
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 6-113 2.91e-03

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 37.09  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860   6 RRWLREAAVFLALLIAIMVVMDVWRAPQAPPAFAATPLHTLTGESTTL-----------ATLSEERPVLLYFWASWCGVC 74
Cdd:COG4232  256 GRRLSVRKGLGLLLLLAGLALLLGALSGADPLQPLAAGAAAAAAAAGLawqadleaalaEARAEGKPVFVDFTADWCVTC 335

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446651860  75 R------FTTPAVARLAAEGenvmTVALRsGD----DAEVARWLARKGV 113
Cdd:COG4232  336 KenertvFSDPEVQAALADD----VVLLK-ADvtdnDPEITALLKRFGR 379
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 43-129 7.55e-03

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 35.03  E-value: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651860  43 LHTLTGESTTLATLSEERPVLLYFW-ASWCGVCRFTTPAVARLAAEGE--NVMTVALrSGDDAEVARWL-ARKGVDFPVV 118
Cdd:cd02970    7 LPDAGGETVTLSALLGEGPVVVVFYrGFGCPFCREYLRALSKLLPELDalGVELVAV-GPESPEKLEAFdKGKFLPFPVY 85

                         90
                 ....*....|.
gi 446651860 119 NDAKGALSAGW 129
Cdd:cd02970   86 ADPDRKLYRAL 96
 
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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