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 1350634634   8 SEVQDILQQSSVAIVYLSMPNCSVCHAVRPRLEELLT-HYDIPALHLDAFETPEVASRFEVLTAPVVLVFHHGKEISRQA 86
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEeYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                          90
                  ....*....|...
gi 1350634634  87 RFIDFKKIRHLLD 99
Cdd:cd02947    81 GADPKEELEEFLE 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 1350634634   8 SEVQDILQQSSVAIVYLSMPNCSVCHAVRPRLEELLT-HYDIPALHLDAFETPEVASRFEVLTAPVVLVFHHGKEISRQA 86
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEeYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                          90
                  ....*....|...
gi 1350634634  87 RFIDFKKIRHLLD 99
Cdd:cd02947    81 GADPKEELEEFLE 93

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1350634634  11 QDILQQSSVAIVYLSMPNCSVCHAVRPRLEELLTHY--DIPALHLDAFETPEVASRFEVLTAPVVLVFHHGKEISRQ 85
Cdd:pfam00085  12 EVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYkgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDY 88

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 1350634634   8 SEVQDILQQSSVAIVYLSMPNCSVCHAVRPRLEELLT-HYDIPALHLDAFETPEVASRFEVLTAPVVLVFHHGKEISRQA 86
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEeYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                          90
                  ....*....|...
gi 1350634634  87 RFIDFKKIRHLLD 99
Cdd:cd02947    81 GADPKEELEEFLE 93

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 1350634634   8 SEVQDILQQ--SSVAIVYLSMPNCSVCHAVRPRLEEL--LTHYDIPALHLDAFETPEVASRFEVLTAPVVLVFHHGKEIS 83
Cdd:cd02984     3 EEFEELLKSdaSKLLVLHFWAPWAEPCKQMNQVFEELakEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVD 82

                  .
gi 1350634634  84 R 84
Cdd:cd02984    83 R 83

Thioredoxin domain-containing protein; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1350634634  27 PNCSVCHAVRPRLEELLTHYD--IPALHLDAFETPEVASRFEVLTAPVVLVFHHGK 80
Cdd:PTZ00443   62 PWCSHCRKMAPAWERLAKALKgqVNVADLDATRALNLAKRFAIKGYPTLLLFDKGK 117