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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  37 VINATGATLDK-LLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKN 115
Cdd:COG3118     2 VVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                          90       100
                  ....*....|....*....|...
gi 1602591415 116 GEVIDMLNGAVPKAPFDSWLNEA 138
Cdd:COG3118    82 GQPVDRFVGALPKEQLREFLDKV 104

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 1602591415  43 ATLDKLLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEErSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKNGEVIDML 122
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                          90
                  ....*....|....
gi 1602591415 123 NGAVPKAPFDSWLN 136
Cdd:cd02947    80 VGADPKEELEEFLE 93

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  37 VINATGATLDK-LLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKN 115
Cdd:COG3118     2 VVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                          90       100
                  ....*....|....*....|...
gi 1602591415 116 GEVIDMLNGAVPKAPFDSWLNEA 138
Cdd:COG3118    82 GQPVDRFVGALPKEQLREFLDKV 104

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 1602591415  43 ATLDKLLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEErSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKNGEVIDML 122
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                          90
                  ....*....|....
gi 1602591415 123 NGAVPKAPFDSWLN 136
Cdd:cd02947    80 VGADPKEELEEFLE 93

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 1602591415  54 PVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKNGEVIDMLNGAVPKAPFDS 133
Cdd:cd02956    14 PVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEEQLRQ 93

                  ...
gi 1602591415 134 WLN 136
Cdd:cd02956    94 MLD 96

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 1602591415  41 TGATLDKLLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEE--RSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKNGE 117
Cdd:cd02961     4 TDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKElkGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGS 82

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 1602591415  45 LDKLLKDDL--PVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKNGEVIDML 122
Cdd:cd02984     5 FEELLKSDAskLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRV 84

                  ....*..
gi 1602591415 123 NGAVPKA 129
Cdd:cd02984    85 SGADPKE 91

disulphide isomerase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  31 DLFDGDVINATGATLDKLLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAE---ERSGKMRFVKVNTEAERELSARFRIRSI 107
Cdd:PTZ00102   28 HFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKmlkEKKSEIVLASVDATEEMELAQEFGVRGY 107

                          90       100       110
                  ....*....|....*....|....*....|
gi 1602591415 108 PTIMMFKNGEVIDmLNGAVPKAPFDSWLNE 137
Cdd:PTZ00102  108 PTIKFFNKGNPVN-YSGGRTADGIVSWIKK 136

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 1602591415  36 DVINATGATLDKLLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEE--RSGKMRFVKVN-TEAERE-LSARFRIRSIPTIM 111
Cdd:cd02997     1 DVVHLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATElkEDGKGVLAAVDcTKPEHDaLKEEYNVKGFPTFK 80

                          90       100
                  ....*....|....*....|....
gi 1602591415 112 MFKNGEVIDMLNGAVPKAPFDSWL 135
Cdd:cd02997    81 YFENGKFVEKYEGERTAEDIIEFM 104

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1602591415  56 VVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSARFRIRSIPTIMMFK 114
Cdd:cd03004    23 LVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYP 81

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 1602591415  37 VINATGATLDKLLKD-DLPVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAE--RELSARFRIRSIPTIMMF 113
Cdd:cd03002     2 VYELTPKNFDKVVHNtNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDknKPLCGKYGVQGFPTLKVF 81

                  .
gi 1602591415 114 K 114
Cdd:cd03002    82 R 82

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 1602591415  52 DLPVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKNGEVIDMLNGAVPKAPF 131
Cdd:cd02949    13 DRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKSEY 92

Thioredoxin domain-containing protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  40 ATGATLDkllkddlPVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSARFRIRSIPTIMMFKNGEVI 119
Cdd:PTZ00443   47 STGATTG-------PWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMY 119

                  ....*
gi 1602591415 120 DMLNG 124
Cdd:PTZ00443  120 QYEGG 124

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 1602591415  35 GDVINATGATLDKLLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEE------RSGKMRFVKVNTEAERELSARFRIRSIP 108
Cdd:cd02996     1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKikeefpDAGKVVWGKVDCDKESDIADRYRINKYP 80

                          90
                  ....*....|.
gi 1602591415 109 TIMMFKNGEVI 119
Cdd:cd02996    81 TLKLFRNGMMM 91

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 1602591415  37 VINATGATLDKLLKDDLP-VVVDFWAPWCGPCRSFAPIFEDVAEERSG--KMRFVKVNTEAErELSARFRIRSIPTIMMF 113
Cdd:cd02995     2 VKVVVGKNFDEVVLDSDKdVLVEFYAPWCGHCKALAPIYEELAEKLKGddNVVIAKMDATAN-DVPSEFVVDGFPTILFF 80

                  ....
gi 1602591415 114 KNGE 117
Cdd:cd02995    81 PAGD 84

disulphide isomerase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  34 DGDVINATGATLDKL-LKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEE--RSGKMRFVKVNTEAERELSARFRIRSIPTI 110
Cdd:PTZ00102  356 DGPVKVVVGNTFEEIvFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKykDNDSIIVAKMNGTANETPLEEFSWSAFPTI 435

                          90
                  ....*....|.
gi 1602591415 111 MMFKNGEVIDM 121
Cdd:PTZ00102  436 LFVKAGERTPI 446

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 1602591415  56 VVDFWAPWCGPCRSFAPIFEDVAEErSGKMRFVKVNT---EAERELSARFRIRSIPTIMMFKNGEVIDM 121
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALL-NKGVKFEAVDVdedPALEKELKRYGVGGVPTLVVFGPGIGVKY 68

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 1602591415  34 DGDVINATGATLDKL-LKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEE-RSGKMRFVKVNTEA-ERELSArFRIRSIPTI 110
Cdd:TIGR01130 345 EGPVKVLVGKNFDEIvLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKyKDAESDVVIAKMDAtANDVPP-FEVEGFPTI 423

                  ....*..
gi 1602591415 111 MMFKNGE 117
Cdd:TIGR01130 424 KFVPAGK 430

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 1602591415  43 ATLDKLLKDDLPVVVDFWAPWCGPCRSFAPIF---EDVAEERSGKMRFVKV----NTEAERELSARFRIRSIPTIMMFKN 115
Cdd:cd02953     2 AALAQALAQGKPVFVDFTADWCVTCKVNEKVVfsdPEVQAALKKDVVLLRAdwtkNDPEITALLKRFGVFGPPTYLFYGP 81

                  .
gi 1602591415 116 G 116
Cdd:cd02953    82 G 82

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  50 KDDLPVVVDFWAPWCGPCR-----SFAPifEDVAEERSGKMRFVKVNTEA-------------ERELSARFRIRSIPTIM 111
Cdd:COG2143    38 AEGKPILLFFESDWCPYCKklhkeVFSD--PEVAAYLKENFVVVQLDAEGdkevtdfdgetltEKELARKYGVRGTPTLV 115

                          90       100
                  ....*....|....*....|....*.
gi 1602591415 112 MF-KNGEVIDMLNGAVPKAPFDSWLN 136
Cdd:COG2143   116 FFdAEGKEIARIPGYLKPETFLALLK 141

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  44 TLDKLLKDDLPVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERELSA--RFRIRSIPTIMMFKN-----G 116
Cdd:cd02950    12 PPEVALSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPEidRYRVDGIPHFVFLDRegneeG 91

                          90
                  ....*....|..
gi 1602591415 117 EVIdmlnGAVPK 128
Cdd:cd02950    92 QSI----GLQPK 99

thiol:disulfide interchange protein precursor; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  54 PVVVDFWAPWCGPCRSFAPI-FEDVA-EERSGKMRFVKV----NTEAERELSARFRIRSIPTIMMF-KNGEVIDML--NG 124
Cdd:PRK00293  476 PVMLDLYADWCVACKEFEKYtFSDPQvQQALADTVLLQAdvtaNNAEDVALLKHYNVLGLPTILFFdAQGQEIPDArvTG 555

                          90
                  ....*....|....
gi 1602591415 125 AVPKAPFDSWLNEA 138
Cdd:PRK00293  556 FMDAAAFAAHLRQL 569

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  54 PVVVDFWAPWCGPCRSFAPIFEDVAEERSGK-MRFVKVNTE---------------------AERELSARFRIRSIPTIM 111
Cdd:COG1225    23 PVVLYFYATWCPGCTAELPELRDLYEEFKDKgVEVLGVSSDsdeahkkfaekyglpfpllsdPDGEVAKAYGVRGTPTTF 102

                          90       100
                  ....*....|....*....|....*....
gi 1602591415 112 MF-KNGEVIDMLNGAVPKAP-FDSWLNEA 138
Cdd:COG1225   103 LIdPDGKIRYVWVGPVDPRPhLEEVLEAL 131

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 1602591415  54 PVVVDFWAPWCGPCRSFAPIFEDVAEERSG-KMRFVKVNTEAERELSARFRIRSIPTIMMFKNGEVIDMLNGAVPK 128
Cdd:cd02963    26 PYLIKITSDWCFSCIHIEPVWKEVIQELEPlGVGIATVNAGHERRLARKLGAHSVPAIVGIINGQVTFYHDSSFTK 101

thioredoxin-like protein

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  59 FWAPWCGPCRSFAPIFEDVaeersgKMRFVKVNTEAERELSARFRIRSIPTIMmfkNGEVIDMLNGaVPK 128
Cdd:PHA02125    5 FGAEWCANCKMVKPMLANV------EYTYVDVDTDEGVELTAKHHIRSLPTLV---NTSTLDRFTG-VPR 64

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  55 VVVDFWAPWCGPCRSFAPI----FEDVAEERSG--------------------KMR---FVKVNTEAERE-LSARFRIRS 106
Cdd:cd02964    20 VGLYFSASWCPPCRAFTPKlvefYEKLKEEGKNfeivfvsrdrseesfneyfsEMPpwlAVPFEDEELRElLEKQFKVEG 99

                          90
                  ....*....|....
gi 1602591415 107 IPTIMMFK-NGEVI 119
Cdd:cd02964   100 IPTLVVLKpDGDVV 113

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
                  ....*....|....*....|....*....|....*....|....*....
gi 1602591415  54 PVVVDFWAPWCGPCRSFAPIFEDVAEErsGKMRFVKVNTEAERELSARF 102
Cdd:cd03010    27 PYLLNVWASWCAPCREEHPVLMALARQ--GRVPIYGINYKDNPENALAW 73

Thioredoxin;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1602591415  47 KLLKDDLPVVVdFWAPWCGPCRSFAPIFEDVAEERSG-KMRFVKvnTEAERELSARFRI---RSIPT-IMMFKNGEVI 119
Cdd:pfam14595  37 KSIEKPLRILV-ITEDWCGDAAQNVPVLAKIAELNPNiELRILL--RDENLELMDQYLTgggRAIPTfIFLDEDGEEL 111

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  16 DDRSADGaKCGRCGHDLFDGD-VINATGATLDKLLKDDL---PVVVDFWAPWCGPCRSFAPIFEDVAEERSGK-MRFVKV 90
Cdd:TIGR00424 332 LDGAVNG-NGSDAVADIFDSNnVVSLSRPGIENLLKLEErkeAWLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKF 410

                          90       100
                  ....*....|....*....|....*
gi 1602591415  91 NTEAERELSAR--FRIRSIPTIMMF 113
Cdd:TIGR00424 411 RADGDQKEFAKqeLQLGSFPTILFF 435

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  37 VINATGATLDKLLKDDLP--VVVDFWAPW----CGPCRSFAPIFEDVA-------EERSGKMRFVKVNTEAERELSARFR 103
Cdd:pfam04756  13 VIKLNDSNYKRLLSGPRDysVVVLLTALDprfgCQLCREFQPEFELVAkswfkdhKAGSSKLFFATLDFDDGKDVFQSLG 92

                          90
                  ....*....|
gi 1602591415 104 IRSIPTIMMF 113
Cdd:pfam04756  93 LQTAPHLLLF 102

thiol-disulfide oxidoreductase ResA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1602591415  55 VVVDFWAPWCGPCRSFAPIFE----------------DVAEERSGKMRFVK-------VNTEAERELSARFRIRSIP-TI 110
Cdd:PRK03147   64 VFLNFWGTWCKPCEKEMPYMNelypkykekgveiiavNVDETELAVKNFVNrygltfpVAIDKGRQVIDAYGVGPLPtTF 143

                          90
                  ....*....|....*...
gi 1602591415 111 MMFKNGEVIDMLNGAVPK 128
Cdd:PRK03147  144 LIDKDGKVVKVITGEMTE 161

Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein located in the ER containing one redox active TRX domain. Denaturation studies indicate that the reduced form is more stable than the oxidized form, suggesting that the protein is involved in disulfide bond formation. In vitro, ERp19 has been shown to possess thiol-disulfide oxidase activity which is dependent on the presence of both active site cysteines. Although described as protein disulfide isomerase (PDI)-like, the protein does not complement for PDI activity. ERp19 shows a wide tissue distribution but is most abundant in liver, testis, heart and kidney.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1602591415  43 ATLDKLLKD----DLPVVVDFWAPWCGPCRSFAPIFEDVAEERSGKMRFVKVNTEAERE 97
Cdd:cd02959     6 VTLEDGIKEakdsGKPLMLLIHKTWCGACKALKPKFAESKEISELSHNFVMVNLEDDEE 64

zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR, pfam12773.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1602591415   1 MNTVCASCQALNRLPDDRSADG---AKCGRCGH 30
Cdd:pfam13717   1 MIITCPSCKAKYRIDDEKIPASgvkVRCSKCGH 33