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 25286717  78 SERDFFQEVKESEK-VVCHFYRDTTFRCKILDRHLAILAKKHLET-KFLKLNVEKAPFLCERLRIKVIPTLALLRDGKTQ 155
Cdd:COG3118   6 TDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEYGGKvKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPV 85

                ....*...
gi 25286717 156 DYVVGFTD 163
Cdd:COG3118  86 DRFVGALP 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25286717    81 DFFQEV--KESEKVVCHFYRDTTFRCKILDRHLAILAKKHLET-KFLKLNVEKAPFLCERLRIKVIPTLALLRDGKTQDY 157
Cdd:pfam00085   8 ANFDEVvqKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNvVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDD 87

                  ...
gi 25286717   158 VVG 160
Cdd:pfam00085  88 YVG 90

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25286717  68 KGHGEYREIgSERDFFQEVKESEK---VVCHFYRDTTFRCKILDRHLAILAKKHLETKFLKLNVEKApFLCERLRIKVIP 144
Cdd:cd02957   1 KGFGEVREI-SSKEFLEEVTKASKgtrVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKA-FLVNYLDIKVLP 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 25286717 145 TLALLRDGKTQDYVVGFTDLGNtDDFTTETLEWRL 179
Cdd:cd02957  79 TLLVYKNGELIDNIVGFEELGG-DDFTTEDLEKFL 112

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 25286717  81 DFFQEVKESEKVVCHFYRDTTFRCKILDRHLAILAKKHLETKFLKLNVEKAPFLCERLRIKVIPTLALLRDGKTQDYVVG 160
Cdd:cd02947   2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVG 81

                .
gi 25286717 161 F 161
Cdd:cd02947  82 A 82

Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein functions. It specifically binds G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane. This impedes the formation of a functional G protein trimer (G protein alphabetagamma), thereby inhibiting G protein-mediated signal transduction. Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25286717  41 EDELELLKEKRLAALRKAQQQK-QEWLSKGH-----GEYREIGSERDFFQEVKESEK---VVCHFYRDTTFRCKILDRHL 111
Cdd:cd02987  26 EQEDDDDDEDKEEFLQQYREQRmQEMHAKLPfgrrfGKVYELDSGEQFLDAIDKEGKdttVVVHIYEPGIPGCAALNSSL 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25286717 112 AILAKKHLETKFLKLNvEKAPFLCERLRIKVIPTLALLRDGKTQDYVVGFT-DLGntDDFTTETLE 176
Cdd:cd02987 106 LCLAAEYPAVKFCKIR-ASATGASDEFDTDALPALLVYKGGELIGNFVRVTeDLG--EDFDAEDLE 168

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 25286717  78 SERDFFQEVKESEK--VVCHFYRDTTFRCKILDRHLAILAKK-HLETKFLKLNVEKAPFLCERLRIKVIPTLALLRDGKT 154
Cdd:cd02984   1 SEEEFEELLKSDASklLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                ....*..
gi 25286717 155 QDYVVGF 161
Cdd:cd02984  81 VDRVSGA 87

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 25286717    78 SERDFFQEVKESEK-VVCHFYRDTTFRCKILDRHLAILAKK-HLETKFLKLNVEKAPFLCERLRIKVIPTLALLRDGKTQ 155
Cdd:TIGR01068   2 TDANFDETIASSDKpVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEV 81

                  ....*.
gi 25286717   156 DYVVGF 161
Cdd:TIGR01068  82 DRSVGA 87

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 25286717  83 FQEVKESEK---VVCHFYRDTTFRCKILDRHLAILAKKHlETKFL--KLNVEKAPFLCERLRIKVIPTLALLRDGKTQD 156
Cdd:cd02956   3 FQQVLQESTqvpVVVDFWAPRSPPSKELLPLLERLAEEY-QGQFVlaKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80