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 896418793   9 QNLTATVESNDIVFLDFWADWCGPCKQFSPVYEAASEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMGFRGGILVYQQA 88
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|..
gi 896418793  89 GALREDQLETVI 100
Cdd:cd02947   81 GADPKEELEEFL 92

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   2 ATIEITQQNLTATVESNDIVFLDFWADWCGPCKQFSPVYEA-ASEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMGFRG 80
Cdd:PRK10996  36 EVINATGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDvAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115

                         90
                 ....*....|....*..
gi 896418793  81 GILVYQQAGALREDQLE 97
Cdd:PRK10996 116 GQVVDMLNGAVPKAPFD 132

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 896418793   9 QNLTATVESNDIVFLDFWADWCGPCKQFSPVYEAASEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMGFRGGILVYQQA 88
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|..
gi 896418793  89 GALREDQLETVI 100
Cdd:cd02947   81 GADPKEELEEFL 92

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   2 ATIEITQQNLTATVESNDIVFLDFWADWCGPCKQFSPVYEA-ASEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMGFRG 80
Cdd:PRK10996  36 EVINATGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDvAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115

                         90
                 ....*....|....*..
gi 896418793  81 GILVYQQAGALREDQLE 97
Cdd:PRK10996 116 GQVVDMLNGAVPKAPFD 132

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 896418793    3 TIEITQQNLTATV-ESNDIVFLDFWADWCGPCKQFSPVYEAASEKHT-DIVFGKVDTEDQGQLAQAAGITSIPTIMGFRG 80
Cdd:pfam00085   2 VVVLTDANFDEVVqKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90
                  ....*....|....*..
gi 896418793   81 GILVYQQAGALREDQLE 97
Cdd:pfam00085  82 GQPVDDYVGARPKDALA 98

disulphide isomerase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   5 EITQQNLTATVESNDIVFLDFWADWCGPCKQFSPVYEAA----SEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMGFRG 80
Cdd:PTZ00102  36 VLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAakmlKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNK 115

                 .
gi 896418793  81 G 81
Cdd:PTZ00102 116 G 116

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793    2 ATIEITQQNLTATVESNDIVFLDFWADWCGPCKQFSPVYEAA----SEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMG 77
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAadelKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90
                  ....*....|
gi 896418793   78 FRGGILVYQQ 87
Cdd:TIGR01130  82 FRNGEDSVSD 91

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   4 IEITQQNLTATV-ESNDIVFLDFWADWCGPCKQFSPVYE---AASEKHTDIVFGKVD-TEDQGQLAQAAGITSIPTIMGF 78
Cdd:cd02998    3 VELTDSNFDKVVgDDKKDVLVEFYAPWCGHCKNLAPEYEklaAVFANEDDVVIAKVDaDEANKDLAKKYGVSGFPTLKFF 82

                 ...
gi 896418793  79 RGG 81
Cdd:cd02998   83 PKG 85

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   9 QNLTATVESND--IVFLDFWADWCGPCKQFSPVYEAASEKHTD-IVFGKVDTEDQGQLAQAAGITSIPTIMGFRGGILVY 85
Cdd:cd02956    1 QNFQQVLQESTqvPVVVDFWAPRSPPSKELLPLLERLAEEYQGqFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|..
gi 896418793  86 QQAGALREDQLE 97
Cdd:cd02956   81 GFQGAQPEEQLR 92

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896418793   4 IEITQQNLTATV-ESNDIVFLDFWADWCGPCKQFSPVYEAASeKHTD--IVFGKVDTEDQGQLAQAAGITSIPTI 75
Cdd:cd03004    4 ITLTPEDFPELVlNRKEPWLVDFYAPWCGPCQALLPELRKAA-RALKgkVKVGSVDCQKYESLCQQANIRAYPTI 77

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793  15 VESNDIVFLDFWADWCGPCKQFSPVYE----AASEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMGFRGGILVYQQAGA 90
Cdd:cd03000   12 VRKEDIWLVDFYAPWCGHCKKLEPVWNevgaELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYNYRGPR 91

                 ....*..
gi 896418793  91 LREDQLE 97
Cdd:cd03000   92 TKDDIVE 98

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   3 TIEITQQNLTATVE-SNDIVFLDFWADWCGPCKQFSPVYE-AASEKHTDIVFGKVDTEDQG--QLAQAAGITSIPTIMGF 78
Cdd:cd03002    2 VYELTPKNFDKVVHnTNYTTLVEFYAPWCGHCKNLKPEYAkAAKELDGLVQVAAVDCDEDKnkPLCGKYGVQGFPTLKVF 81

                         90
                 ....*....|
gi 896418793  79 RGGILVYQQA 88
Cdd:cd03002   82 RPPKKASKHA 91

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   9 QNLTATVESNDI----VFLDFWADWCGPCKQFSPVYEA-ASEKHTDIV---------------------FGKVDTEDQGQ 62
Cdd:cd03010   12 PGPDKTLTSADLkgkpYLLNVWASWCAPCREEHPVLMAlARQGRVPIYginykdnpenalawlarhgnpYAAVGFDPDGR 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 896418793  63 LAQAAGITSIPT--IMGfRGGILVYQQAGALREDQLE 97
Cdd:cd03010   92 VGIDLGVYGVPEtfLID-GDGIIRYKHVGPLTPEVWE 127

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 896418793  16 ESNDIVFLDFWADWCGPCKQFSPVY-EAASEKHTDIVFGKVDTEDQGQLAQAAGITSIPTIMGFRGGILVYQQAG 89
Cdd:cd02949   11 ESDRLILVLYTSPTCGPCRTLKPILnKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 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 896418793   2 ATIEITQQNLTATVeSNDIVFLDFWADWCGPCKQFSPVYE--AASEKH--TDIVFGKVD-TEDQgQLAQAAGITSIPTIM 76
Cdd:cd03005    1 GVLELTEDNFDHHI-AEGNHFVKFFAPWCGHCKRLAPTWEqlAKKFNNenPSVKIAKVDcTQHR-ELCSEFQVRGYPTLL 78

                 ....*
gi 896418793  77 GFRGG 81
Cdd:cd03005   79 LFKDG 83

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   6 ITQQNLTATVESNDIVFLDFWADWCGPCKQFSPVYEAASE---KHTDIVFGKVDTEDQGQ--LAQAAGITSIPTIMGFRG 80
Cdd:cd02997    5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATelkEDGKGVLAAVDCTKPEHdaLKEEYNVKGFPTFKYFEN 84

                 ....*.
gi 896418793  81 GILVYQ 86
Cdd:cd02997   85 GKFVEK 90

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   4 IEITQQNLTATVESNDIVflDFWADWCGPCKQFSPVYEAASEKHTD--IVFGKVDTEDQGQLAQAAGITSIPTIMGFRGG 81
Cdd:cd02994    4 VELTDSNWTLVLEGEWMI--EFYAPWCPACQQLQPEWEEFADWSDDlgINVAKVDVTQEPGLSGRFFVTALPTIYHAKDG 81

                 .
gi 896418793  82 I 82
Cdd:cd02994   82 V 82

thiol-disulfide oxidoreductase ResA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793  21 VFLDFWADWCGPCKQFSP----VYEAASEKHTDIVFGKVDTED--------------------QGQLAQAAGITSIP-TI 75
Cdd:PRK03147  64 VFLNFWGTWCKPCEKEMPymneLYPKYKEKGVEIIAVNVDETElavknfvnrygltfpvaidkGRQVIDAYGVGPLPtTF 143

                         90       100
                 ....*....|....*....|....*....
gi 896418793  76 MGFRGGILVYQQAGALREDQLETVIGSIR 104
Cdd:PRK03147 144 LIDKDGKVVKVITGEMTEEQLEEYLEKIK 172

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793  21 VFLDFWADWCGPCKQFSPVYEAASEKHTD---IVFG-KVDTEDQ-------------------GQLAQAAGITSIPTIMG 77
Cdd:COG1225   24 VVLYFYATWCPGCTAELPELRDLYEEFKDkgvEVLGvSSDSDEAhkkfaekyglpfpllsdpdGEVAKAYGVRGTPTTFL 103

                         90       100
                 ....*....|....*....|....*
gi 896418793  78 F-RGGILVYQQAGALRED-QLETVI 100
Cdd:COG1225  104 IdPDGKIRYVWVGPVDPRpHLEEVL 128

disulphide isomerase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896418793  21 VFLDFWADWCGPCKQFSPVYEAASEKHTD---IVFGKVDTEDQGQLAQAAGITSIPTIMGFRGG 81
Cdd:PTZ00102 378 VLLEIYAPWCGHCKNLEPVYNELGEKYKDndsIIVAKMNGTANETPLEEFSWSAFPTILFVKAG 441

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 896418793   4 IEITQQNLTATV-ESNDIVFLDFWADWCGPCKQFSPVYEAASEK 46
Cdd:cd02992    4 IVLDAASFNSALlGSPSAWLVEFYASWCGHCRAFAPTWKKLARD 47

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896418793  25 FWADWCGPCKQFSPVYEAASEK--HTDIVFGKVDTEDQGQLAQAAGITS------IPTIMGFRGG 81
Cdd:cd02962   54 FFTTWSPECVNFAPVFAELSLKynNNNLKFGKIDIGRFPNVAEKFRVSTsplskqLPTIILFQGG 118

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 896418793  13 ATVESNDI----VFLDFWADWCGPCKQFSP----VYEAASEKHTD--IVF 52
Cdd:cd03009    9 GKVPVSSLegktVGLYFSASWCPPCRAFTPklveFYEKLKESGKNfeIVF 58

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793   21 VFLDFWADWCGPCKQFSPVYEAASEKHTDIVfgKVDTEDQ-----------------------GQLAQAAGITSIP-TIM 76
Cdd:TIGR00385  66 VLLNVWASWCPPCRAEHPYLNELAKQGLPIV--GVDYKDDrqnaikflkelgnpyqlslfdpdGMLGLDLGVYGAPeTFL 143

                          90       100
                  ....*....|....*....|....
gi 896418793   77 GFRGGILVYQQAGALREDQLETVI 100
Cdd:TIGR00385 144 VDGNGVIRYRHAGPLNPEVWTEEF 167

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896418793  16 ESNDIVFLDFWADWCGPCKQFSPVYEAASEKHTDIVFGKV---DTEDQGQLAQAAGITSIPTIMGFRGGILVYQQAGALR 92
Cdd:cd02985   13 AKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDGEKIHEEEGIGP 92

                         90
                 ....*....|.
gi 896418793  93 eDQLetvIGSI 103
Cdd:cd02985   93 -DEL---IGDV 99