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 767956860  10 EFKTFLTAAghKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKVI 89
Cdd:cd02947    2 EFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|.
gi 767956860  90 SGIYKAKEVRS 100
Cdd:cd02947   80 VGADPKEELEE 90

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 767956860  10 EFKTFLTAAghKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKVI 89
Cdd:cd02947    2 EFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|.
gi 767956860  90 SGIYKAKEVRS 100
Cdd:cd02947   80 VGADPKEELEE 90

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 767956860   1 MVQIIKDTNeFKTFLTAAgHKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQN-VFFANVDVNNSPELAETCHIKTIPTFQM 79
Cdd:COG3118    1 AVVELTDEN-FEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLL 78

                         90       100
                 ....*....|....*....|
gi 767956860  80 FKKSQKYKVISGIYKAKEVR 99
Cdd:COG3118   79 FKDGQPVDRFVGALPKEQLR 98

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 767956860   10 EFKTFLtAAGHKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQN-VFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKV 88
Cdd:TIGR01068   5 NFDETI-ASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGkVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDR 83

                  ...
gi 767956860   89 ISG 91
Cdd:TIGR01068  84 SVG 86

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 767956860  10 EFKTFLTAAghKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKVI 89
Cdd:cd02947    2 EFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|.
gi 767956860  90 SGIYKAKEVRS 100
Cdd:cd02947   80 VGADPKEELEE 90

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 767956860   1 MVQIIKDTNeFKTFLTAAgHKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQN-VFFANVDVNNSPELAETCHIKTIPTFQM 79
Cdd:COG3118    1 AVVELTDEN-FEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLL 78

                         90       100
                 ....*....|....*....|
gi 767956860  80 FKKSQKYKVISGIYKAKEVR 99
Cdd:COG3118   79 FKDGQPVDRFVGALPKEQLR 98

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 767956860  10 EFKTFLTAAGHKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQ-NVFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKV 88
Cdd:cd02984    4 EFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFpSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDR 83

                         90
                 ....*....|..
gi 767956860  89 ISGIyKAKEVRS 100
Cdd:cd02984   84 VSGA-DPKELAK 94

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 767956860  21 KLAVVQFSSKRCGPCKRMFPVFHAMSVKYQN-VFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKVISGIYKAKEVR 99
Cdd:cd02949   14 RLILVLYTSPTCGPCRTLKPILNKVIDEFDGaVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKSEYR 93

thioredoxin 2; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956860  24 VVQFSSKRCGPCKRMFPVFHAMSVKYQ-NVFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKVISG 91
Cdd:PRK10996  56 VIDFWAPWCGPCRNFAPIFEDVAAERSgKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNG 124

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767956860  11 FKTFLTAAGHKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVF-FANVDVNNSPELAETCHIKTIPTFQMFKKSQ 84
Cdd:cd02956    3 FQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFvLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQ 77

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767956860  21 KLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVNNSPELAE 67
Cdd:COG0526   29 KPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAVK 75

Thioredoxin domain-containing protein; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767956860  25 VQFSSKRCGPCKRMFPVFHAMSVKYQNVF-FANVDVNNSPELAETCHIKTIPTFQMFKKSQKYKVISG 91
Cdd:PTZ00443  57 VKFYAPWCSHCRKMAPAWERLAKALKGQVnVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGG 124

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 767956860  27 FSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVNNSPELAET---CHIKTIPTFQMFKKSQKYKV 88
Cdd:cd01659    4 FYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKElkrYGVGGVPTLVVFGPGIGVKY 68

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767956860  24 VVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVNNSPELAETCHIKTIPTFQMFKKSQ 84
Cdd:cd02989   26 VCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVILFKNGK 86

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767956860  21 KLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDV 59
Cdd:cd03023    6 DVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEF 44