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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894    6 LTAAQFNETIQSSD-MVLVDYWASWCGPCRAFAPTFAE-SSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKL 83
Cdd:TIGR01068   1 LTDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEElAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90       100
                  ....*....|....*....|.
gi 339330894   84 LFNQAGALPPAALESLVQQLK 104
Cdd:TIGR01068  81 VDRSVGALPKAALKQLINKNL 101

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894    6 LTAAQFNETIQSSD-MVLVDYWASWCGPCRAFAPTFAE-SSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKL 83
Cdd:TIGR01068   1 LTDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEElAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90       100
                  ....*....|....*....|.
gi 339330894   84 LFNQAGALPPAALESLVQQLK 104
Cdd:TIGR01068  81 VDRSVGALPKAALKQLINKNL 101

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 339330894   9 AQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAESSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKLLFNQA 88
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|...
gi 339330894  89 GALPPAALESLVQ 101
Cdd:cd02947   81 GADPKEELEEFLE 93

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   7 TAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAE-SSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKLLF 85
Cdd:PRK10996  41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDvAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120

                         90
                 ....*....|....*..
gi 339330894  86 NQAGALPPAALESLVQQ 102
Cdd:PRK10996 121 MLNGAVPKAPFDSWLNE 137

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894    6 LTAAQFNETIQSSD-MVLVDYWASWCGPCRAFAPTFAE-SSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKL 83
Cdd:TIGR01068   1 LTDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEElAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90       100
                  ....*....|....*....|.
gi 339330894   84 LFNQAGALPPAALESLVQQLK 104
Cdd:TIGR01068  81 VDRSVGALPKAALKQLINKNL 101

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 339330894   9 AQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAESSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKLLFNQA 88
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|...
gi 339330894  89 GALPPAALESLVQ 101
Cdd:cd02947   81 GADPKEELEEFLE 93

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   7 TAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAE-SSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKLLF 85
Cdd:PRK10996  41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDvAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120

                         90
                 ....*....|....*..
gi 339330894  86 NQAGALPPAALESLVQQ 102
Cdd:PRK10996 121 MLNGAVPKAPFDSWLNE 137

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   5 DLTAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTF---AESSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNG 81
Cdd:cd02961    2 ELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYeklAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNG 81

                 .
gi 339330894  82 K 82
Cdd:cd02961   82 S 82

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 339330894    6 LTAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAES----SEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNG 81
Cdd:TIGR01130   6 LTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAadelKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNG 85

                  .
gi 339330894   82 K 82
Cdd:TIGR01130  86 E 86

disulphide isomerase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   5 DLTAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTF----AESSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKN 80
Cdd:PTZ00102  36 VLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYkkaaKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNK 115

                         90       100
                 ....*....|....*....|...
gi 339330894  81 GKLLfNQAGALPPAALESLVQQL 103
Cdd:PTZ00102 116 GNPV-NYSGGRTADGIVSWIKKL 137

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 339330894   2 TTRDLTAAQFNETIQSSDmVLVDYWASWCGPCRAFAPTFAESSEKH----PDVVHAKVDTEAERELAAAAQIRSIPTIMA 77
Cdd:cd03005    1 GVLELTEDNFDHHIAEGN-HFVKFFAPWCGHCKRLAPTWEQLAKKFnnenPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                 ....*
gi 339330894  78 FKNGK 82
Cdd:cd03005   80 FKDGE 84

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   6 LTAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAESS----EKHPD---VVHAKVDTEAERELAAAAQIRSIPTIMAF 78
Cdd:cd02996    6 LTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAakikEEFPDagkVVWGKVDCDKESDIADRYRINKYPTLKLF 85

                 ....*
gi 339330894  79 KNGKL 83
Cdd:cd02996   86 RNGMM 90

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   6 LTAAQFNETI-QSSDMVLVDYWASWCGPCRAFAPTF---AESSEKHPDVVHAKVDtEAERELAAAAQIRSIPTIMAFKNG 81
Cdd:cd02995    5 VVGKNFDEVVlDSDKDVLVEFYAPWCGHCKALAPIYeelAEKLKGDDNVVIAKMD-ATANDVPSEFVVDGFPTILFFPAG 83

                 .
gi 339330894  82 K 82
Cdd:cd02995   84 D 84

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   7 TAAQFNETIQS--SDMVLVDYWASWCGPCRAFAPTFAE-SSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKL 83
Cdd:cd02984    1 SEEEFEELLKSdaSKLLVLHFWAPWAEPCKQMNQVFEElAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                         90
                 ....*....|.
gi 339330894  84 LFNQAGALPPA 94
Cdd:cd02984   81 VDRVSGADPKE 91

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 339330894   6 LTAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAESSE---KHPDVVHAKVDTEAERELAAAAQ--IRSIPTIMAFKN 80
Cdd:cd02997    5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATelkEDGKGVLAAVDCTKPEHDALKEEynVKGFPTFKYFEN 84

                 ....*.
gi 339330894  81 GKLLFN 86
Cdd:cd02997   85 GKFVEK 90

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 339330894    6 LTAAQFNETIQSSDM-VLVDYWASWCGPCRAFAPTFAESSEKH----PDVVHAKVDteAERELAAAAQIRSIPTIMAFKN 80
Cdd:TIGR01130 351 LVGKNFDEIVLDETKdVLVEFYAPWCGHCKNLAPIYEELAEKYkdaeSDVVIAKMD--ATANDVPPFEVEGFPTIKFVPA 428

                  ..
gi 339330894   81 GK 82
Cdd:TIGR01130 429 GK 430

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 339330894  13 ETIQSSDM----VLVDYWASWCGPCRAFAPTFAESSEKHPD 49
Cdd:cd02966   10 KPVSLSDLkgkvVLVNFWASWCPPCRAEMPELEALAKEYKD 50

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
                 ....*....|....*....|....*....|....*....|....*....
gi 339330894   2 TTRDLTAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAESSEKHPDV 50
Cdd:cd03011    4 TATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYPVV 52

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
                 ....*....|....*....|....*..
gi 339330894  21 VLVDYWASWCGPCRAFAPTFAESSEKH 47
Cdd:cd03009   21 VGLYFSASWCPPCRAFTPKLVEFYEKL 47

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 339330894   5 DLTA-AQFNETIQSSDM----VLVDYWASWCGPCRAFAPTFAESSEKHPD 49
Cdd:COG1225    3 DFTLpDLDGKTVSLSDLrgkpVVLYFYATWCPGCTAELPELRDLYEEFKD 52

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

                          10        20        30
                  ....*....|....*....|....*....|.
gi 339330894   19 DMVLVDYWASWCGPCRAFAPTFAESSEKHPD 49
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYEKLKK 32

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 339330894   6 LTAAQFNETIQSSD-MVLVDYWASWCGPCRAFAPTFAE-SSEKHPDVVHAKVDTEAERELAAAAQ--IRSIPTIMAFKNG 81
Cdd:cd03002    5 LTPKNFDKVVHNTNyTTLVEFYAPWCGHCKNLKPEYAKaAKELDGLVQVAAVDCDEDKNKPLCGKygVQGFPTLKVFRPP 84

                 .
gi 339330894  82 K 82
Cdd:cd03002   85 K 85

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
                 ....*....|....*....
gi 339330894  21 VLVDYWASWCGPCRAFAPT 39
Cdd:cd03010   28 YLLNVWASWCAPCREEHPV 46

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 339330894  16 QSSDMVLVDYWASWCGPCRAFAPTFAESSEKHPDVVH-AKVDTEAERELAAAAQIRSIPTIMAFKNGKLL 84
Cdd:cd02949   11 ESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHfVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELV 80

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894  20 MVLVDYWASWCGPCRAF------APTFAESSEKHPDVVHAKVD-----------TEAERELAAAAQIRSIPTIMAF-KNG 81
Cdd:COG2143   42 PILLFFESDWCPYCKKLhkevfsDPEVAAYLKENFVVVQLDAEgdkevtdfdgeTLTEKELARKYGVRGTPTLVFFdAEG 121

                         90       100
                 ....*....|....*....|...
gi 339330894  82 KLLFNQAGALPPAALESLVQQLK 104
Cdd:COG2143  122 KEIARIPGYLKPETFLALLKYVA 144

Thioredoxin-like domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339330894   21 VLVDYWASWCGPCRAFAPTF-----------AESSEKH------PDVVHAKVDTEAERELAAAAQIRSIPTImAFKNGKL 83
Cdd:pfam13098   7 VLVVFTDPDCPYCKKLKKELledpdvtvylgPNFVFIAvniwcaKEVAKAFTDILENKELGRKYGVRGTPTI-VFFDGKG 85

                          90
                  ....*....|....*..
gi 339330894   84 LFNQA-GALPPAALESL 99
Cdd:pfam13098  86 ELLRLpGYVPAEEFLAL 102