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 654962034   8 EQYKEVIKEGK-HIMMFSADWCPDCRVIEPVLPEIEANHSEYTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEETGRFV 86
Cdd:cd02947    1 EEFEELIKSAKpVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|....*
gi 654962034  87 SKDrkTKEEIEEFIN 101
Cdd:cd02947   81 GAD--PKEELEEFLE 93

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 654962034   8 EQYKEVIKEGK-HIMMFSADWCPDCRVIEPVLPEIEANHSEYTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEETGRFV 86
Cdd:cd02947    1 EEFEELIKSAKpVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|....*
gi 654962034  87 SKDrkTKEEIEEFIN 101
Cdd:cd02947   81 GAD--PKEELEEFLE 93

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962034    6 TIEQYKEVIKEGKHIMM--FSADWCPDCRVIEPVLPEIEAN-HSEYTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEET 82
Cdd:TIGR01068   2 TDANFDETIASSDKPVLvdFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEV 81

                          90
                  ....*....|....*....
gi 654962034   83 GRFVSKdrKTKEEIEEFIN 101
Cdd:TIGR01068  82 DRSVGA--LPKAALKQLIN 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 654962034    6 TIEQYKEVIKEGKHIMM--FSADWCPDCRVIEPVLPEIEANHSE-YTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEET 82
Cdd:pfam00085   6 TDANFDEVVQKSSKPVLvdFYAPWCGPCKMLAPEYEELAQEYKGnVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPV 85

                          90
                  ....*....|....*....
gi 654962034   83 GRFVSkdRKTKEEIEEFIN 101
Cdd:pfam00085  86 DDYVG--ARPKDALAAFLK 102

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 654962034   8 EQYKEVIKEGK-HIMMFSADWCPDCRVIEPVLPEIEANHSEYTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEETGRFV 86
Cdd:cd02947    1 EEFEELIKSAKpVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                         90
                 ....*....|....*
gi 654962034  87 SKDrkTKEEIEEFIN 101
Cdd:cd02947   81 GAD--PKEELEEFLE 93

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962034    6 TIEQYKEVIKEGKHIMM--FSADWCPDCRVIEPVLPEIEAN-HSEYTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEET 82
Cdd:TIGR01068   2 TDANFDETIASSDKPVLvdFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEV 81

                          90
                  ....*....|....*....
gi 654962034   83 GRFVSKdrKTKEEIEEFIN 101
Cdd:TIGR01068  82 DRSVGA--LPKAALKQLIN 98

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962034   3 KMQTIEQYKevikeGK-HIMMFSADWCPDCRVIEPVLPEIEANHSEYTFHYVDRDDFID--------------------- 60
Cdd:COG0526   19 KPLSLADLK-----GKpVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEavkaflkelglpypvlldpdg 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 654962034  61 -LCAELSIFGIPSFVGY-SNGEETGRFVSkdRKTKEEIEEFINGL 103
Cdd:COG0526   94 eLAKAYGVRGIPTTVLIdKDGKIVARHVG--PLSPEELEEALEKL 136

Thioredoxin;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962034   14 IKEGKHIMMFSADWCPDCRVIEPVLPEIEANHSEYTFHYVDRDDFIDLCAELSIFG---IPSFVGY-SNGEETGRFVSKD 89
Cdd:pfam14595  39 IEKPLRILVITEDWCGDAAQNVPVLAKIAELNPNIELRILLRDENLELMDQYLTGGgraIPTFIFLdEDGEELGVWGPRP 118

                          90
                  ....*....|
gi 654962034   90 RKTKEEIEEF 99
Cdd:pfam14595 119 KAVQELVDEA 128

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 654962034   9 QYKEVIKEGKHIMM-FSADWCPDCRVIEPVLPEIEANHSE---YTFHYVDRDDFIDLCAELSIFGIPSFVGYSN-GEETG 83
Cdd:cd02950   12 PPEVALSNGKPTLVeFYADWCTVCQEMAPDVAKLKQKYGDqvnFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDReGNEEG 91

                         90       100
                 ....*....|....*....|
gi 654962034  84 RFVSkdRKTKEEIEEFINGL 103
Cdd:cd02950   92 QSIG--LQPKQVLAQNLDAL 109

thioredoxin TrxA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962034  12 EVIK-EGKHIMMFSADWCPDCRVIEPVLPEI-EANHSEYTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEETGRFVSKd 89
Cdd:PRK09381  16 DVLKaDGAILVDFWAEWCGPCKMIAPILDEIaDEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGA- 94

                         90
                 ....*....|...
gi 654962034  90 rKTKEEIEEFING 102
Cdd:PRK09381  95 -LSKGQLKEFLDA 106

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 654962034   8 EQYKEVIKEGKHIMM-FSADWCPDCRVIEPVL---PEIEAnhsEYTFHYV-------DRDDFID-LCAELSIFGIPSFVG 75
Cdd:cd02953    2 AALAQALAQGKPVFVdFTADWCVTCKVNEKVVfsdPEVQA---ALKKDVVllradwtKNDPEITaLLKRFGVFGPPTYLF 78

                 ....*.
gi 654962034  76 YSNGEE 81
Cdd:cd02953   79 YGPGGE 84

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962034   5 QTIEQYKeviKEGKHIMM-FSADWCPDCRVIE-------PVLPEIEANhseytFHYV-----DRDDFI-DLCAELSIFGI 70
Cdd:COG4232  311 AALAEAR---AEGKPVFVdFTADWCVTCKENErtvfsdpEVQAALADD-----VVLLkadvtDNDPEItALLKRFGRFGV 382

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654962034  71 PSFVGYS-NGEETGRFVSKdrKTKEEIEEFINGLNA 105
Cdd:COG4232  383 PTYVFYDpDGEELPRLGFM--LTADEFLAALEKAKG 416

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 654962034   8 EQYKEVIKEGKHI-MMFSADWCPDCRVIEPVL---PEIEANHSEYTFHYVD--RDDFIDLCAELSIFGIPSFVGYSNGEE 81
Cdd:cd02997    8 EDFRKFLKKEKHVlVMFYAPWCGHCKKMKPEFtkaATELKEDGKGVLAAVDctKPEHDALKEEYNVKGFPTFKYFENGKF 87

                         90
                 ....*....|....*....
gi 654962034  82 tgRFVSKDRKTKEEIEEFI 100
Cdd:cd02997   88 --VEKYEGERTAEDIIEFM 104

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 654962034   6 TIEQYKEVIKEGKH---IMMFSADWCPDCRVIEPVLPEI-EANHSEYTFHYVDRDDFIDLCAELSIFGIPSFVGYSNGEE 81
Cdd:cd02984    1 SEEEFEELLKSDASkllVLHFWAPWAEPCKQMNQVFEELaKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                 ...
gi 654962034  82 TGR 84
Cdd:cd02984   81 VDR 83

Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the Actinobacteria and contains the conserved CxxC motif.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 654962034   19 HIMMFSADWCPDCRVIEPVLpeiEANHSEYTFHYVDRD 56
Cdd:TIGR02200   1 TITVYGTTWCGYCAQLMRTL---DKLGAAYEWVDIEED 35