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 1309125295  12 ERFRKDVVDPSQtsLVILDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQP 91
Cdd:COG3118     8 ENFEEEVLESDK--PVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                          90       100
                  ....*....|....*....|.
gi 1309125295  92 VADLTSARTETQLKAAIDQLL 112
Cdd:COG3118    85 VDRFVGALPKEQLREFLDKVL 105

Tetratricopeptide repeat;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309125295 148 AGDPQRAASIFAQITEFAPENAPAHAGLVRALVQLGEVDQAHQVMQVIDADPRLAADPAMTAAK 211
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64

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 1309125295  12 ERFRKDVVDPSQtsLVILDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQP 91
Cdd:COG3118     8 ENFEEEVLESDK--PVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                          90       100
                  ....*....|....*....|.
gi 1309125295  92 VADLTSARTETQLKAAIDQLL 112
Cdd:COG3118    85 VDRFVGALPKEQLREFLDKVL 105

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 1309125295  22 SQTSLVILDFWAEWCGPCKALTPVLEKVAGEYADkgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQPVADLTSARTE 101
Cdd:cd02947     8 KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADPK 85

                  ....*...
gi 1309125295 102 TQLKAAID 109
Cdd:cd02947    86 EELEEFLE 93

thioredoxin 2; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  27 VILDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQPVADLTSARTETQLKA 106
Cdd:PRK10996   55 VVIDFWAPWCGPCRNFAPIFEDVAAERSGK-VRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGAVPKAPFDS 133

                  ....*.
gi 1309125295 107 AIDQLL 112
Cdd:PRK10996  134 WLNEAL 139

Tetratricopeptide repeat;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309125295 148 AGDPQRAASIFAQITEFAPENAPAHAGLVRALVQLGEVDQAHQVMQVIDADPRLAADPAMTAAK 211
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64

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 1309125295  12 ERFRKDVVDPSQtsLVILDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQP 91
Cdd:COG3118     8 ENFEEEVLESDK--PVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                          90       100
                  ....*....|....*....|.
gi 1309125295  92 VADLTSARTETQLKAAIDQLL 112
Cdd:COG3118    85 VDRFVGALPKEQLREFLDKVL 105

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 1309125295  22 SQTSLVILDFWAEWCGPCKALTPVLEKVAGEYADkgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQPVADLTSARTE 101
Cdd:cd02947     8 KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADPK 85

                  ....*...
gi 1309125295 102 TQLKAAID 109
Cdd:cd02947    86 EELEEFLE 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 1309125295  17 DVVDPSQTSLVILDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQPVADLT 96
Cdd:cd02956     5 QVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQ-FVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQ 83

                          90
                  ....*....|...
gi 1309125295  97 SARTETQLKAAID 109
Cdd:cd02956    84 GAQPEEQLRQMLD 96

Tetratricopeptide repeat;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295 220 RVDDGELATLRAAAVANPADMDAQFAFAEAAFAAGSRDEAADTLLAMVAADREWNEGAARTQLLKIFEATGLEDEWVIGV 299
Cdd:pfam14561   2 AADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAKY 81

                  ....*....
gi 1309125295 300 RRRLSRVLF 308
Cdd:pfam14561  82 RRKLSSLLF 90

thioredoxin TrxA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  12 ERFRKDVVDPSQTSLVilDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQP 91
Cdd:PRK09381   11 DSFDTDVLKADGAILV--DFWAEWCGPCKMIAPILDEIADEYQGK-LTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEV 87

                          90
                  ....*....|....*...
gi 1309125295  92 VADLTSARTETQLKAAID 109
Cdd:PRK09381   88 AATKVGALSKGQLKEFLD 105

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 1309125295  16 KDVVDPSQTSLVilDFWAEWCGPCKALTPVLEKVAGEYADKG-VVLAKVNVDEEQFIAAQFQVRSIPTVY 84
Cdd:cd02961     9 DELVKDSKDVLV--EFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDCTANNDLCSEYGVRGYPTIK 76

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309125295  14 FRKDVVDPSQTSLVilDFWAEWCGPCKALTPVLEKVAGEYA-DKGVVLAKVNVDEEQF-IAAQFQVRSIPTVY 84
Cdd:cd02998    10 FDKVVGDDKKDVLV--EFYAPWCGHCKNLAPEYEKLAAVFAnEDDVVIAKVDADEANKdLAKKYGVSGFPTLK 80

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  25 SLVILDFWAEWCGPCKALTPVLEKVAGEYadKGVV-LAKVNVDEEQFIAAQFQVRSIPTV 83
Cdd:cd03001    19 DVWLVEFYAPWCGHCKNLAPEWKKAAKAL--KGIVkVGAVDADVHQSLAQQYGVRGFPTI 76

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309125295  14 FRKDVVDPSQTslVILDFWAEWCGPCKALTPVLEKVAGEYAD--KGVVLAKVNVDEEQfiAAQFQVRSIPTVY 84
Cdd:TIGR01130 356 FDEIVLDETKD--VLVEFYAPWCGHCKNLAPIYEELAEKYKDaeSDVVIAKMDATAND--VPPFEVEGFPTIK 424

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 1309125295  12 ERFRKDVVDPSQTSLVilDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTV 83
Cdd:cd03004     9 EDFPELVLNRKEPWLV--DFYAPWCGPCQALLPELRKAARALKGK-VKVGSVDCQKYESLCQQANIRAYPTI 77

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 1309125295  31 FWAEWCGPCKALTPVLEKVAGEY--ADKGVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQPVADLTSARTETQLKA 106
Cdd:cd03005    23 FFAPWCGHCKRLAPTWEQLAKKFnnENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGTRDLDSLKE 100

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 1309125295  14 FRKDVVDPSQTSLVIldFWAEWCGPCKALTPVLEKVAGEyADKGVVLAKVNVDEEQF--IAAQFQVRSIPTVyAMFQGQP 91
Cdd:cd03002    10 FDKVVHNTNYTTLVE--FYAPWCGHCKNLKPEYAKAAKE-LDGLVQVAAVDCDEDKNkpLCGKYGVQGFPTL-KVFRPPK 85

                  ..
gi 1309125295  92 VA 93
Cdd:cd03002    86 KA 87

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 1309125295  12 ERFRKdVVDPSQTSLVILDFWAEWCGPCKALTPVLEKVAGEYaDKGVVLAKVNVDEEQFIAAQFQVRSIPTVYAMFQGQP 91
Cdd:cd02984     3 EEFEE-LLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEA-FPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                  ....*..
gi 1309125295  92 VADLTSA 98
Cdd:cd02984    81 VDRVSGA 87

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  10 AVERFRKDVVDPSQTSLVILDFWAEWCGPCKALTPVLEKVAGEYADKG--VVLAKVNVDEEQFIAAQFQVRSIPTVyAMF 87
Cdd:cd03000     1 LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGspVRVGKLDATAYSSIASEFGVRGYPTI-KLL 79

                          90
                  ....*....|....*..
gi 1309125295  88 QGQPVADLTSARTETQL 104
Cdd:cd03000    80 KGDLAYNYRGPRTKDDI 96

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309125295  31 FWAEWCGPCKALTPVLEKVAGEYADKG-VVLAKVNVDEEQF--IAAQFQVRSIPTVYAMFQGQPVADLTSARTE 101
Cdd:cd02997    24 FYAPWCGHCKKMKPEFTKAATELKEDGkGVLAAVDCTKPEHdaLKEEYNVKGFPTFKYFENGKFVEKYEGERTA 97

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1309125295  26 LVILDFWAEWCGPCKALTPVLEKVAGEYADKgVVLAKVNVDEEQFIAAQFQVRSIPTV 83
Cdd:cd02949    15 LILVLYTSPTCGPCRTLKPILNKVIDEFDGA-VHFVEIDIDEDQEIAEAAGIMGTPTV 71

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 1309125295  28 ILDFWAEWCGPCKALTPVLEKVAGEYADK-GVVLakVNVDEEQFIAA--QFQVRSIPTvYAMF--QGQPVADLTSARTET 102
Cdd:cd02950    24 LVEFYADWCTVCQEMAPDVAKLKQKYGDQvNFVM--LNVDNPKWLPEidRYRVDGIPH-FVFLdrEGNEEGQSIGLQPKQ 100

                          90
                  ....*....|.
gi 1309125295 103 QLKAAIDQLLT 113
Cdd:cd02950   101 VLAQNLDALVA 111

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  25 SLVILDFWAEWCGPCKALTPVLEKVAGEYADKG----VVLAKVNVDEEQF----------------------IAAQFQVR 78
Cdd:cd03009    19 KTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGknfeIVFISWDRDEESFndyfskmpwlavpfsdrerrsrLNRTFKIE 98

                  ....*
gi 1309125295  79 SIPTV 83
Cdd:cd03009    99 GIPTL 103

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 1309125295  26 LVILDFWAEWCGPCKALTPVLEKVAGEY-ADKGVVLAKVNVD--EEQF-----------------------IAAQFQVRS 79
Cdd:pfam13905   3 VVLLYFGASWCKPCRRFTPLLKELYEKLkKKKNVEIVFVSLDrdLEEFkdylkkmpkdwlsvpfddderneLKRKYGVNA 82

                  ....*
gi 1309125295  80 IPTVY 84
Cdd:pfam13905  83 IPTLV 87

Tetratricopeptide repeat;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309125295 148 AGDPQRAASIFAQITEFAPENAPAHAGLVRALVQLGEVDQAHQVMQVIDADPRLAADPAMTAAK 211
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  27 VILDFWAEWCGPCKAL------TPVLEKvageYADKGVVLAKVNVD--------------EEQFiAAQFQVRSIPTVyaM 86
Cdd:COG2143    43 ILLFFESDWCPYCKKLhkevfsDPEVAA----YLKENFVVVQLDAEgdkevtdfdgetltEKEL-ARKYGVRGTPTL--V 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 1309125295  87 F---QGQPVADLTSARTETQLKAAIDQLLT 113
Cdd:COG2143   116 FfdaEGKEIARIPGYLKPETFLALLKYVAE 145

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295 131 SPEEIAQFIKLGDEALSAGDPQRAASIFAQITEFAPENAPAHAGLVRALVQLGEVDQA-HQVMQVIDADPrlaadpamTA 209
Cdd:COG2956    72 DPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAiEVLERLLKLGP--------EN 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295 210 AKSALELAGTRVDDGE----LATLRAAAVANPADMDAQFAFAEAAFAAGSRDEAADTLLAMVAADREWneGAARTQLLKI 285
Cdd:COG2956   144 AHAYCELAELYLEQGDydeaIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY--LPALPRLAEL 221

                         170
                  ....*....|.
gi 1309125295 286 FEATGLEDEWV 296
Cdd:COG2956   222 YEKLGDPEEAL 232

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295 133 EEIAQFIKLGDEALSAGDPQRAASIFAQITEFAPENAPAHAGLVRALVQLGEVDQAHQVMQ-VIDADPrlaaDPAMTAAK 211
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHeALELDP----DEPEARLN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1309125295 212 SALELAGTRVDDGELATLRAAAVANPADMDAQFAFAEAAFAAGSRDEAADTLLAMVAAD 270
Cdd:COG4783    78 LGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295 132 PEEIAQFIKLGDEALSAGDPQRAASIFAQITEFAPENAPAHAGLVRALVQLGEVDQA-HQVMQVIDADPRLAA------- 203
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAiAALRRALELDPDNAEalnnlgn 188

                          90       100
                  ....*....|....*....|..
gi 1309125295 204 --------DPAMTAAKSALELA 217
Cdd:COG3914   189 alqdlgrlEEAIAAYRRALELD 210

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
                  ....*....|....*....|....*....|
gi 1309125295  23 QTSLVILDFWAEWCGPCKALTPVLEKVAGE 52
Cdd:TIGR00385  62 QGKPVLLNVWASWCPPCRAEHPYLNELAKQ 91

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  26 LVILdfWAEWCGPCKALTPVLEKVAGEYADKGVVLAKVNVDEEQ--FIAAQFQVRSIPTV 83
Cdd:TIGR00424 375 LVVL--YAPWCPFCQAMEASYLELAEKLAGSGVKVAKFRADGDQkeFAKQELQLGSFPTI 432

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295  27 VILDFWAEWCGPCKAL-------TPVLEKVAgeyadKGVVLAKVNVD--EEQFIA--AQFQVRSIPTvYAMF--QGQPVA 93
Cdd:COG4232   323 VFVDFTADWCVTCKENertvfsdPEVQAALA-----DDVVLLKADVTdnDPEITAllKRFGRFGVPT-YVFYdpDGEELP 396

                          90
                  ....*....|....*....
gi 1309125295  94 DLTSARTETQLKAAIDQLL 112
Cdd:COG4232   397 RLGFMLTADEFLAALEKAK 415

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1309125295  27 VILDFWAE-WCGPCKALTPVLEKVAGEYADKGVVLAKVNVDEE 68
Cdd:pfam00578  28 VVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSP 70

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309125295 131 SPEEIAQFIKLGDEALSAGDPQRAASIFAQITEFAPENAPAHAGLVRALVQLGEVDQAHQVM-QVIDADPRlaadpamtA 209
Cdd:COG2956   106 DPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALeKALKLDPD--------C 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309125295 210 AKSALELAGTRVDDGE----LATLRAAAVANPADMDAQFAFAEAAFAAGSRDEAADTLLAMVAAD 270
Cdd:COG2956   178 ARALLLLAELYLEQGDyeeaIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELD 242