Calsequestrin;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854   68 LEMKSIGspvkVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQ---QMFE 144
Cdd:pfam01216  63 LEDKDIG----FGLVDAEKDAALAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGElelQAFE 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767998854  145 HMQKRHRVFFVYVGGESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLK 195
Cdd:pfam01216 139 NIEDEIKLIGFFKSEDSEHYKAFEDAAEEFHPYIKFFATFDKGVAKKLSLK 189

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854   32 DESFKENRNDD-IWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGsPVKVGKMDATSYSSIASEFGVRGYPTIKLL-KGDL 109
Cdd:TIGR01126   3 ASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDP-KIVLAKVDATAEKDLASRFGVSGFPTIKFFpKGSK 81

                          90
                  ....*....|....*..
gi 767998854  110 AYNYRGPRTKDDIIEFA 126
Cdd:TIGR01126  82 PVDYEGGRDLEAIVEFV 98

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854   32 DESFKE--NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKsigSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GD 108
Cdd:pfam00085   7 DANFDEvvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK---GNVVFAKVDVDENPDLASKYGVRGYPTLIFFKnGQ 83

                          90
                  ....*....|....*..
gi 767998854  109 LAYNYRGPRTKDDIIEF 125
Cdd:pfam00085  84 PVDDYVGARPKDALAAF 100

Calsequestrin;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854   68 LEMKSIGspvkVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQ---QMFE 144
Cdd:pfam01216  63 LEDKDIG----FGLVDAEKDAALAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGElelQAFE 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767998854  145 HMQKRHRVFFVYVGGESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLK 195
Cdd:pfam01216 139 NIEDEIKLIGFFKSEDSEHYKAFEDAAEEFHPYIKFFATFDKGVAKKLSLK 189

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 767998854  32 DESFKE-NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSiGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKG--D 108
Cdd:cd02961    5 DDNFDElVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG-DGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNgsK 83

                         90
                 ....*....|....*...
gi 767998854 109 LAYNYRGPRTKDDIIEFA 126
Cdd:cd02961   84 EPVKYEGPRTLESLVEFI 101

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 767998854  28 VEDLDESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKLL 105
Cdd:cd03001    3 VELTDSNFDKKvlNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGI---VKVGAVDADVHQSLAQQYGVRGFPTIKVF 79

                         90       100
                 ....*....|....*....|...
gi 767998854 106 KGDL--AYNYRGPRTKDDIIEFA 126
Cdd:cd03001   80 GAGKnsPQDYQGGRTAKAIVSAA 102

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 767998854  33 ESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GDLAY 111
Cdd:cd03005    8 DNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKdGEKVD 87

                         90
                 ....*....|....
gi 767998854 112 NYRGPRTKDDIIEF 125
Cdd:cd03005   88 KYKGTRDLDSLKEF 101

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854   32 DESFKE--NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKsigSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GD 108
Cdd:pfam00085   7 DANFDEvvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK---GNVVFAKVDVDENPDLASKYGVRGYPTLIFFKnGQ 83

                          90
                  ....*....|....*..
gi 767998854  109 LAYNYRGPRTKDDIIEF 125
Cdd:pfam00085  84 PVDDYVGARPKDALAAF 100

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854  28 VEDL-DESFKENRNDDIW--LVDFYAPWCGHCKKLEPIWNEVGLEMKSiGSPVKVGKMDAT-SYSSIASEFGVRGYPTIK 103
Cdd:cd02998    2 VVELtDSNFDKVVGDDKKdvLVEFYAPWCGHCKNLAPEYEKLAAVFAN-EDDVVIAKVDADeANKDLAKKYGVSGFPTLK 80

                         90       100
                 ....*....|....*....|....
gi 767998854 104 LL-KGDLA-YNYRGPRTKDDIIEF 125
Cdd:cd02998   81 FFpKGSTEpVKYEGGRDLEDLVKF 104

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 767998854  32 DESFKENRNDDI-WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGkMDATS--YSSIASEFGVRGYPTIKLL-KG 107
Cdd:cd02997    7 DEDFRKFLKKEKhVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAA-VDCTKpeHDALKEEYNVKGFPTFKYFeNG 85

                         90
                 ....*....|....*...
gi 767998854 108 DLAYNYRGPRTKDDIIEF 125
Cdd:cd02997   86 KFVEKYEGERTAEDIIEF 103

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854  26 GFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGspVKVGKMDATSYSSIASEFGVRGYPTIKLL 105
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLG--INVAKVDVTQEPGLSGRFFVTALPTIYHA 78

                         90       100
                 ....*....|....*....|
gi 767998854 106 KGDLAYNYRGPRTKDDIIEF 125
Cdd:cd02994   79 KDGVFRRYQGPRDKEDLISF 98

Thioredoxin domain-containing protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854  44 WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYR-GPRTKDDI 122
Cdd:PTZ00443  55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEgGDRSTEKL 131

                         90
                 ....*....|....*...
gi 767998854 123 IEFA-HRVSGALIRPLPS 139
Cdd:PTZ00443 132 AAFAlGDFKKALGAPVPA 149

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 767998854  45 LVDFYAPWCGHCKKLEPIWNEVGlemKSIGSPVKVGKM--DATSYSSIASEFGVRGYPTIKLLK------GDLAYNYRGP 116
Cdd:cd03002   22 LVEFYAPWCGHCKNLKPEYAKAA---KELDGLVQVAAVdcDEDKNKPLCGKYGVQGFPTLKVFRppkkasKHAVEDYNGE 98

                         90
                 ....*....|
gi 767998854 117 RTKDDIIEFA 126
Cdd:cd03002   99 RSAKAIVDFV 108

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 767998854  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKSigspVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GDLAYNYRGPRTKDDII 123
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDVDENPELAEEYGVRSIPTFLFFKnGKEVDRVVGADPKEELE 89

                 ..
gi 767998854 124 EF 125
Cdd:cd02947   90 EF 91

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854  40 NDDIWLVDFYAPWCGHCKKLEPIWNEvgleMKSIGSPVKVGKMDATS-YSSIASEFGVRGYPTIKLLKGDLAYNYRGPRT 118
Cdd:cd02999   17 REDYTAVLFYASWCPFSASFRPHFNA----LSSMFPQIRHLAIEESSiKPSLLSRYGVVGFPTILLFNSTPRVRYNGTRT 92

                 ....*..
gi 767998854 119 KDDIIEF 125
Cdd:cd02999   93 LDSLAAF 99

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854  42 DIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAY-NYRGPRTKD 120
Cdd:cd03003   19 EIWFVNFYSPRCSHCHDLAPTWREFAKEMDGV---IRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGMNPeKYYGDRSKE 95

                 ....*.
gi 767998854 121 DIIEFA 126
Cdd:cd03003   96 SLVKFA 101

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 767998854  39 RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSI---GSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYN--Y 113
Cdd:cd02996   16 QSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpdAGKVVWGKVDCDKESDIADRYRINKYPTLKLFRNGMMMKreY 95

                         90
                 ....*....|..
gi 767998854 114 RGPRTKDDIIEF 125
Cdd:cd02996   96 RGQRSVEALAEF 107

thioredoxin 2; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998854  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVgkmDATSYSSIASEFGVRGYPTIKLLK 106
Cdd:PRK10996  56 VIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKV---NTEAERELSARFRIRSIPTIMIFK 114

thioredoxin; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998854  41 DDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSigspVKVGKMDATSYSSIASEFGVRGYPTIKLLK 106
Cdd:PTZ00051  18 NELVIVDFYAEWCGPCKRIAPFYEECSKEYTK----MVFVKVDVDELSEVAEKENITSMPTFKVFK 79

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 767998854   37 ENRNDDiWLVDFYAPWCGHCKKLEPIWNEvgLEMKSIGSPVKVGKM--DATSYSSIASEFGVRGYPTIKLLKGDLAYNYR 114
Cdd:TIGR00424 368 EERKEA-WLVVLYAPWCPFCQAMEASYLE--LAEKLAGSGVKVAKFraDGDQKEFAKQELQLGSFPTILFFPKHSSRPIK 444

                  ....*...
gi 767998854  115 GPRTKDDI 122
Cdd:TIGR00424 445 YPSEKRDV 452

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854  31 LDESFKEnrnddIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGspVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLA 110
Cdd:cd02963   19 VPKSFKK-----PYLIKITSDWCFSCIHIEPVWKEVIQELEPLG--VGIATVNAGHERRLARKLGAHSVPAIVGIINGQV 91

                         90       100
                 ....*....|....*....|
gi 767998854 111 YNYR-GPRTKDDIIEFAHRV 129
Cdd:cd02963   92 TFYHdSSFTKQHVVDFVRKL 111

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998854  45 LVDFYAPWCGHCKKLEPIWNevGLEMKSIGSPVkVGKMDATSYSSIASEFGVRGYPTIKLLKG 107
Cdd:cd02956   16 VVDFWAPRSPPSKELLPLLE--RLAEEYQGQFV-LAKVNCDAQPQIAQQFGVQALPTVYLFAA 75

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 767998854  40 NDDIWLVDFYAPWCGHCKKLEPIWNEVgleMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKG-DLAYNYRGPRT 118
Cdd:cd02949   12 SDRLILVLYTSPTCGPCRTLKPILNKV---IDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDkELVKEISGVKM 88

                 ....*..
gi 767998854 119 KDDIIEF 125
Cdd:cd02949   89 KSEYREF 95

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998854  45 LVDFYAPWCGHCKKLEPI-------WNEVGLEMKSiGSPVKVGK-MDATSY---------SSIASEFGVRGYPTIKLLKG 107
Cdd:cd03011   24 LVYFWATWCPVCRFTSPTvnqlaadYPVVSVALRS-GDDGAVARfMQKKGYgfpvindpdGVISARWGVSVTPAIVIVDP 102

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gi 767998854 108 D 108
Cdd:cd03011  103 G 103