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 268324174   51 LTDDTFMDAVRKS-SLIVVDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDENPKVATDFAIMAIPTMFIFKNGEP 129
Cdd:TIGR01068   1 LTDANFDETIASSdKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90       100
                  ....*....|....*....|.
gi 268324174  130 VDVIQGALPKpyleAKLKEWL 150
Cdd:TIGR01068  81 VDRSVGALPK----AALKQLI 97

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 268324174  54 DTFMDAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEYaGKVVFGKLNVDENPKVATDFAIMAIPTMFIFKNGEPVDVI 133
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|....
gi 268324174 134 QGALPKPYLEAKLK 147
Cdd:cd02947   80 VGADPKEELEEFLE 93

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 268324174   51 LTDDTFMDAVRKS-SLIVVDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDENPKVATDFAIMAIPTMFIFKNGEP 129
Cdd:TIGR01068   1 LTDANFDETIASSdKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90       100
                  ....*....|....*....|.
gi 268324174  130 VDVIQGALPKpyleAKLKEWL 150
Cdd:TIGR01068  81 VDRSVGALPK----AALKQLI 97

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 268324174  54 DTFMDAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEYaGKVVFGKLNVDENPKVATDFAIMAIPTMFIFKNGEPVDVI 133
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|....
gi 268324174 134 QGALPKPYLEAKLK 147
Cdd:cd02947   80 VGADPKEELEEFLE 93

thioredoxin TrxA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  46 DYPLTLTDDTF-MDAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDENPKVATDFAIMAIPTMFIF 124
Cdd:PRK09381   3 DKIIHLTDDSFdTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82

                         90       100
                 ....*....|....*....|....*.
gi 268324174 125 KNGEPVDVIQGALPKpyleAKLKEWL 150
Cdd:PRK09381  83 KNGEVAATKVGALSK----GQLKEFL 104

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 268324174  49 LTLTDDTFMDAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEYA--GKVVFGKLNVDENPKVATDFAIMAIPTMFIFKN 126
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                 ..
gi 268324174 127 GE 128
Cdd:cd02961   81 GS 82

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  66 IVVDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGkLNVDENP----------------------KVATDFAIMAIPTMFI 123
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVG-VDVDENPeavkaflkelglpypvlldpdgELAKAYGVRGIPTTVL 109

                         90       100
                 ....*....|....*....|....*...
gi 268324174 124 F-KNGEPVDVIQGALPKPYLEAKLKEWL 150
Cdd:COG0526  110 IdKDGKIVARHVGPLSPEELEEALEKLL 137

disulphide isomerase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  39 EQKEGIIDYPLTLTDDTFMDAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEYA---GKVVFGKLNVDENPKVATDFAI 115
Cdd:PTZ00102  25 AEEHFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGV 104

                         90
                 ....*....|....*.
gi 268324174 116 MAIPTMFIFKNGEPVD 131
Cdd:PTZ00102 105 RGYPTIKFFNKGNPVN 120

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  51 LTDDTFMDAVRKSSLIV-VDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDENPKVATDFAIMAIPTMFIFKNG-- 127
Cdd:cd03001    5 LTDSNFDKKVLNSDDVWlVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGAGkn 84

                 ....
gi 268324174 128 EPVD 131
Cdd:cd03001   85 SPQD 88

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 268324174  50 TLTDDTFMDAVRKSSLI-VVDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDENPKVATDFAIMAIPTMFIFK 125
Cdd:cd03004    5 TLTPEDFPELVLNRKEPwLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYP 81

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 268324174  47 YPLTLTDDTFMDAVrKSSLIVVDCWAPWCGPCKTIAPVIEELAKEY---AGKVVFGKLNVDENPKVATDFAIMAIPTMFI 123
Cdd:cd03005    1 GVLELTEDNFDHHI-AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                         90
                 ....*....|...
gi 268324174 124 FKNGEPVDVIQGA 136
Cdd:cd03005   80 FKDGEKVDKYKGT 92

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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  66 IVVDCWAPWCGPCKTIAPVIEELAKEYAGK--VVFGkLNVDENP-----------------------KVATDFAIMAIPT 120
Cdd:cd02966   22 VLVNFWASWCPPCRAEMPELEALAKEYKDDgvEVVG-VNVDDDDpaavkaflkkygitfpvlldpdgELAKAYGVRGLPT 100

                         90
                 ....*....|....*.
gi 268324174 121 MFIF-KNGEPVDVIQG 135
Cdd:cd02966  101 TFLIdRDGRIRARHVG 116

Thioredoxin domain-containing protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  51 LTDDTFMDAVRKSSLIVVDCW-----APWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDENPKVATDFAIMAIPTMFIFK 125
Cdd:PTZ00443  35 LNDKNFEKLTQASTGATTGPWfvkfyAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFD 114

                 ...
gi 268324174 126 NGE 128
Cdd:PTZ00443 115 KGK 117

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  49 LTLTDdTFMDAVRKSSL----IVVDCWAPWCGPCKTIAPVIEELAKEYAGK--VVFG--------------KLNV----- 103
Cdd:COG1225    4 FTLPD-LDGKTVSLSDLrgkpVVLYFYATWCPGCTAELPELRDLYEEFKDKgvEVLGvssdsdeahkkfaeKYGLpfpll 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 268324174 104 -DENPKVATDFAIMAIPTMFIF-KNGEPVDVIQGAL-PKPYLEAKLKEWL 150
Cdd:COG1225   83 sDPDGEVAKAYGVRGTPTTFLIdPDGKIRYVWVGPVdPRPHLEEVLEALL 132

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268324174  67 VVDCWAPWCGPCKTIAPVIEELAKEYAGkVVFGKLNVDENP---KVATDFAIMAIPTMFIFKNGEPVDV 132
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEDPaleKELKRYGVGGVPTLVVFGPGIGVKY 68

disulphide isomerase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  14 EEAEIEQIKERKMREMEERIKARGEEQKEgiiDYPLT-LTDDTFMDAVRKSSL-IVVDCWAPWCGPCKTIAPVIEELAKE 91
Cdd:PTZ00102 327 VEALIEFFKDVEAGKVEKSIKSEPIPEEQ---DGPVKvVVGNTFEEIVFKSDKdVLLEIYAPWCGHCKNLEPVYNELGEK 403

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 268324174  92 YA--GKVVFGKLNVDENPKVATDFAIMAIPTMFIFKNGE 128
Cdd:PTZ00102 404 YKdnDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGE 442

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268324174  49 LTLTDDTFMDAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDENPKVATDFAIMAIPTMFIFKNG 127
Cdd:cd03003    4 VTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG 82

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  51 LTDDTFMDAVRKSSLI--VVDCWAPWCGPCKTIAPVIEELAKEYAGKVV-FGKLNVDENPKVATDFAIMA------IPTM 121
Cdd:cd02962   33 FTPKTLEEELERDKRVtwLVEFFTTWSPECVNFAPVFAELSLKYNNNNLkFGKIDIGRFPNVAEKFRVSTsplskqLPTI 112

                         90
                 ....*....|
gi 268324174 122 FIFKNGEPVD 131
Cdd:cd02962  113 ILFQGGKEVA 122

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 268324174  51 LTDDTFMDAVRKSS-LIVVDCWAPWCGPCKTIAPVIEELAKEYAGKVVFGKLNVDE--NPKVATDFAIMAIPTMFIFKNG 127
Cdd:cd03002    5 LTPKNFDKVVHNTNyTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEdkNKPLCGKYGVQGFPTLKVFRPP 84

                 ...
gi 268324174 128 EPV 130
Cdd:cd03002   85 KKA 87

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 268324174   75 CGPCKTIAPVIEELAKEYA-------GKVVFGKLNVDENPKVATDFAIMAIPTMFIF 124
Cdd:pfam04756  46 CQLCREFQPEFELVAKSWFkdhkagsSKLFFATLDFDDGKDVFQSLGLQTAPHLLLF 102

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  56 FMDAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEYAGkVVFGKLNVDENPKVATDFAIMAIPTMFIFKNGEPVDVIQG 135
Cdd:cd02989   15 FFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLE-TKFIKVNAEKAPFLVEKLNIKVLPTVILFKNGKTVDRIVG 93

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268324174  62 KSSLIVVDCWAPWCGPCKTIAPVIEELAKEyAGKVVFGKLNVDENPK---VATDFAIMAIPTMFIFKNGEPV 130
Cdd:cd02985   14 KGRLVVLEFALKHSGPSVKIYPTMVKLSRT-CNDVVFLLVNGDENDStmeLCRREKIIEVPHFLFYKDGEKI 84

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174   65 LIVVDCWAPWCGPCKTIAPVIEELAKEYAGK----VVFgkLNVDE-----------NPKVATDFA--------------I 115
Cdd:pfam13905   3 VVLLYFGASWCKPCRRFTPLLKELYEKLKKKknveIVF--VSLDRdleefkdylkkMPKDWLSVPfdddernelkrkygV 80

                          90
                  ....*....|....
gi 268324174  116 MAIPTMFIF-KNGE 128
Cdd:pfam13905  81 NAIPTLVLLdPNGE 94

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 268324174   58 DAVRKSSLIVVDCWAPWCGPCKTIAPVIEELAKEY-----------AGKVV---------FGKLNVDENPKVATDFAIMA 117
Cdd:TIGR00385  58 DVLTQGKPVLLNVWASWCPPCRAEHPYLNELAKQGlpivgvdykddRQNAIkflkelgnpYQLSLFDPDGMLGLDLGVYG 137

                  ....*.
gi 268324174  118 IPTMFI 123
Cdd:TIGR00385 138 APETFL 143

5'-adenylylsulfate reductase

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268324174  61 RKSSLIVVdCWAPWCGPCKTIAPVIEELAKEYAGK-VVFGKLNVDENPKvatDFA-----IMAIPTMFIFKNGEP 129
Cdd:PLN02309 364 RKEPWLVV-LYAPWCPFCQAMEASYEELAEKLAGSgVKVAKFRADGDQK---EFAkqelqLGSFPTILLFPKNSS 434

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 268324174  62 KSSLIVVdcWAPWCGPCKTIAPVIEELAKEYAG-KVVFGKLNVD 104
Cdd:cd02993   22 QSTLVVL--YAPWCPFCQAMEASYEELAEKLAGsNVKVAKFNAD 63

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268324174  59 AVRKSSLIVVDCWAPWCGPCKTIAPVI---EELAKEYAGKVVFGKLNV-DENPKVA---TDFAIMAIPTMFIF--KNGEP 129
Cdd:cd02953    7 ALAQGKPVFVDFTADWCVTCKVNEKVVfsdPEVQAALKKDVVLLRADWtKNDPEITallKRFGVFGPPTYLFYgpGGEPE 86

                         90
                 ....*....|....*...
gi 268324174 130 VDVIQGALPKPYLEAKLK 147
Cdd:cd02953   87 PLRLPGFLTADEFLEALE 104