Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179910165  27 FVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd03000     1 LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKL 78

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179910165  27 FVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd03000     1 LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKL 78

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179910165  32 DESFKENRNDD-IWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGsPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:TIGR01126   3 ASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDP-KIVLAKVDATAEKDLASRFGVSGFPTIKF 75

disulphide isomerase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165  24 CKGFVEDLDESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPT 101
Cdd:PTZ00102   30 ISEHVTVLTDSTFDKfiTENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165 102 IKL----------------ALIR-----PLPSQQMFE------HMQKRHRVFFV--YVGGESPLKEKYIDAAS---ELIV 149
Cdd:PTZ00102  110 IKFfnkgnpvnysggrtadGIVSwikklTGPAVTEVEsaseikLIAKKIFVAFYgeYTSKDSELYKKFEEVADkhrEHAK 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165 150 YTYFFSASEEVVpeYVTLKEMPAVLVFKDETYFVYDEY---EDGDLSSWINRERFQNYLAMDGFLLYELGdtgklvalav 226
Cdd:PTZ00102  190 FFVKKHEGKNKI--YVLHKDEEGVELFMGKTKEELEEFvstESFPLFAEINAENYRRYISSGKDLVWFCG---------- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165 227 ideknTSVEHTRLKSIIQEVARDYRDLFHrdFQFGHMD--GNDYINTLLMDELtvPTVVVlNTSNQQYFLLDRQIK--NV 302
Cdd:PTZ00102  258 -----TTEDYDKYKSVVRKVARKLREKYA--FVWLDTEqfGSHAKEHLLIEEF--PGLAY-QSPAGRYLLPPAKESfdSV 327

                         330
                  ....*....|....*.
gi 1179910165 303 EDMVQFINNILDGTVE 318
Cdd:PTZ00102  328 EALIEFFKDVEAGKVE 343

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179910165  32 DESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMksiGSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:COG3118     7 DENFEEEvlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY---GGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165 230 KNTSVEHTRLKSIIQEVARDYRDLFHrdfqFGHMDGNDY---INTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMV 306
Cdd:cd02982    21 NKDDSESEELRERFKEVAKKFKGKLL----FVVVDADDFgrhLEYFGLKEEDLPVIAIINLSDGKKYLMPEEELTAESLE 96

                  ....*..
gi 1179910165 307 QFINNIL 313
Cdd:cd02982    97 EFVEDFL 103

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179910165  27 FVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd03000     1 LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKL 78

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179910165  32 DESFKE-NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSiGSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd02961     5 DDNFDElVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG-DGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179910165  32 DESFKENRNDD-IWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGsPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:TIGR01126   3 ASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDP-KIVLAKVDATAEKDLASRFGVSGFPTIKF 75

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1179910165  33 ESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd03005     8 DNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179910165  32 DESFKE--NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKsigSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:pfam00085   7 DANFDEvvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK---GNVVFAKVDVDENPDLASKYGVRGYPTLIF 78

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165  28 VEDLD-ESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd03004     3 VITLTpEDFPELvlNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGK---VKVGSVDCQKYESLCQQANIRAYPTIRL 79

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1179910165  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSsiASEFGVRGYPTIKLA 105
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATAND--VPPFEVEGFPTIKFV 426

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179910165  32 DESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMksiGSPVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:COG3118     7 DENFEEEvlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY---GGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78

Thioredoxin domain-containing protein; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1179910165  44 WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:PTZ00443   55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAKRFAIKGYPTLLL 112

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179910165  26 GFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGspVKVGKMDATSYSSIASEFGVRGYPTI 102
Cdd:cd02994     1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLG--INVAKVDVTQEPGLSGRFFVTALPTI 75

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKSigspVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd02947    14 VVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDVDENPELAEEYGVRSIPTFLF 69

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        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1179910165  44 WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIA--SEFGVRGYPTIK 103
Cdd:cd02992    22 WLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVAlcRDFGVTGYPTLR 83

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1179910165  42 DIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTI 102
Cdd:cd03003    19 EIWFVNFYSPRCSHCHDLAPTWREFAKEMDGV---IRIGAVNCGDDRMLCRSQGVNSYPSL 76

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179910165  40 NDDIWLVDFYAPWCGHCKKLEPIWNevglEMKSIGSPVKVGKMDATS-YSSIASEFGVRGYPTIKLA 105
Cdd:cd02999    17 REDYTAVLFYASWCPFSASFRPHFN----ALSSMFPQIRHLAIEESSiKPSLLSRYGVVGFPTILLF 79

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 1179910165  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKsigsPVKVGKMDATSYSSI---ASEFGVRGYPTIKL 104
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNK----GVKFEAVDVDEDPALekeLKRYGVGGVPTLVV 59

thioredoxin; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179910165  41 DDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSigspVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:PTZ00051   18 NELVIVDFYAEWCGPCKRIAPFYEECSKEYTK----MVFVKVDVDELSEVAEKENITSMPTFKV 77

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165  40 NDDIWLVDFYAPWCGHCKKLEPIWNEV-----GLEMKSI---GSPVKVGK------MDATSY----SSIASEFGVRGYPT 101
Cdd:COG0526    27 KGKPVLVNFWATWCPPCRAEMPVLKELaeeygGVVFVGVdvdENPEAVKAflkelgLPYPVLldpdGELAKAYGVRGIPT 106

                  .
gi 1179910165 102 I 102
Cdd:COG0526   107 T 107

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1179910165  31 LDESFKEnrnddIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGspVKVGKMDATSYSSIASEFGVRGYPTI 102
Cdd:cd02963    19 VPKSFKK-----PYLIKITSDWCFSCIHIEPVWKEVIQELEPLG--VGIATVNAGHERRLARKLGAHSVPAI 83

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165  27 FVEDLDESFKENRNddIwLVDFYAPWCGHCKKLEpiwNEVgLEMKSIGSPVK----VGKMDA-------------TSYSS 89
Cdd:COG2143    29 LEEDLALAKAEGKP--I-LLFFESDWCPYCKKLH---KEV-FSDPEVAAYLKenfvVVQLDAegdkevtdfdgetLTEKE 101

                          90
                  ....*....|...
gi 1179910165  90 IASEFGVRGYPTI 102
Cdd:COG2143   102 LARKYGVRGTPTL 114

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910165  40 NDDIWLVDFYAPWCGHCKKLEPIWNEVgleMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLALIRPLPSQQMFEHM 119
Cdd:cd02949    12 SDRLILVLYTSPTCGPCRTLKPILNKV---IDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKM 88

                  ....*...
gi 1179910165 120 QKRHRVFF 127
Cdd:cd02949    89 KSEYREFI 96