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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457   8 ESFKSVINSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQYNDYQWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKIAHLH 87
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|....*
gi 613174457  88 SANAKspEQVESFLA 102
Cdd:cd02947   81 GADPK--EELEEFLE 93

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457   8 ESFKSVINSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQYNDYQWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKIAHLH 87
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|....*
gi 613174457  88 SANAKspEQVESFLA 102
Cdd:cd02947   81 GADPK--EELEEFLE 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457    6 SNESFKSVI-NSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQY-NDYQWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKI 83
Cdd:pfam00085   6 TDANFDEVVqKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPV 85

                          90       100
                  ....*....|....*....|
gi 613174457   84 AHLHSANAKspEQVESFLAE 103
Cdd:pfam00085  86 DDYVGARPK--DALAAFLKA 103

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457   8 ESFKSVINSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQYNDYQWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKIAHLH 87
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|....*
gi 613174457  88 SANAKspEQVESFLA 102
Cdd:cd02947   81 GADPK--EELEEFLE 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457    6 SNESFKSVI-NSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQY-NDYQWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKI 83
Cdd:pfam00085   6 TDANFDEVVqKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPV 85

                          90       100
                  ....*....|....*....|
gi 613174457   84 AHLHSANAKspEQVESFLAE 103
Cdd:pfam00085  86 DDYVGARPK--DALAAFLKA 103

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457  19 PVIVKFEAGWCPDCRAMDLWIDPIVEQYNDYQWYTVNRDELED--------------VVVENE--------VMGIPSLLV 76
Cdd:COG0526   30 PVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEavkaflkelglpypVLLDPDgelakaygVRGIPTTVL 109

                         90       100
                 ....*....|....*....|....*..
gi 613174457  77 FKNGDKIAHLHsANAKSPEQVESFLAE 103
Cdd:COG0526  110 IDKDGKIVARH-VGPLSPEELEEALEK 135

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457   6 SNESFKSVINSDTPVIVKFEAGWCPDCRAM-DLWIDPIVEQYNDYQWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKIA 84
Cdd:PRK10996  41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFaPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120

                         90       100
                 ....*....|....*....|
gi 613174457  85 HLHSANAKSPeqVESFLAET 104
Cdd:PRK10996 121 MLNGAVPKAP--FDSWLNEA 138

thioredoxin TrxA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457   6 SNESFKS-VINSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQYN-DYQWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKI 83
Cdd:PRK09381   9 TDDSFDTdVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVA 88

                         90
                 ....*....|....*...
gi 613174457  84 AhlHSANAKSPEQVESFL 101
Cdd:PRK09381  89 A--TKVGALSKGQLKEFL 104

TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613174457  16 SDTPVIVKFEAGWCPDCRAMDLWIDPIVEQYNDY-QWYTVNRDELEDVVVENEVMGIPSLLVFKNGDKIAHLHSANAKS 93
Cdd:cd02949   12 SDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAvHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKS 90

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613174457  14 INSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQYND---YQWYTVNRDELEDVVVENEVMGIPSLLVFKN 79
Cdd:cd02950   17 LSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDqvnFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDR 85

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457   6 SNESFKSVInSDTPVIVKFEAGWCPDCRAMDlwidPIVEQYNDYQwytvnRDELEDVVV-------------ENEVMGIP 72
Cdd:cd03005    6 TEDNFDHHI-AEGNHFVKFFAPWCGHCKRLA----PTWEQLAKKF-----NNENPSVKIakvdctqhrelcsEFQVRGYP 75

                         90
                 ....*....|.
gi 613174457  73 SLLVFKNGDKI 83
Cdd:cd03005   76 TLLLFKDGEKV 86

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174457   8 ESFKSVINSDTPVIVKFEAGWCPDCRAMDLWIDPIVEQYN---------------------DYQWYTVNrDELEDVVVEN 66
Cdd:cd03011   11 EQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYPvvsvalrsgddgavarfmqkkGYGFPVIN-DPDGVISARW 89

                         90
                 ....*....|....*.
gi 613174457  67 EVMGIPSLLVFKNGDK 82
Cdd:cd03011   90 GVSVTPAIVIVDPGGI 105

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

                         10        20
                 ....*....|....*....|....
gi 613174457  11 KSVINSDTPVIVKFEAGWCPDCRA 34
Cdd:PRK14018  50 SVYLKKDKPTLIKFWASWCPLCLS 73