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 1365260310   8 EELASFVKREGKIVFFFTAEWCGDCRFIKPFLPEIEAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQEIGRFV 87
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                          90
                  ....*....|....*
gi 1365260310  88 NreRKTKTQINEFLA 102
Cdd:cd02947    81 G--ADPKEELEEFLE 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 1365260310   8 EELASFVKREGKIVFFFTAEWCGDCRFIKPFLPEIEAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQEIGRFV 87
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                          90
                  ....*....|....*
gi 1365260310  88 NreRKTKTQINEFLA 102
Cdd:cd02947    81 G--ADPKEELEEFLE 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 1365260310  15 KREGKIVFFFTAEWCGDCRFIKPFLPEIEAENP-DFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQEIGRFVnrERKT 93
Cdd:pfam00085  16 KSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYV--GARP 93

                  ....*....
gi 1365260310  94 KTQINEFLA 102
Cdd:pfam00085  94 KDALAAFLK 102

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1365260310  24 FTAEWCGDCRFIKP----FLPEIEAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENG 80
Cdd:TIGR01130  25 FYAPWCGHCKSLAPeyekAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNG 85

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 1365260310   8 EELASFVKREGKIVFFFTAEWCGDCRFIKPFLPEIEAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQEIGRFV 87
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                          90
                  ....*....|....*
gi 1365260310  88 NreRKTKTQINEFLA 102
Cdd:cd02947    81 G--ADPKEELEEFLE 93

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310  18 GKIVF-FFTAEWCGDCRFIKPFLPEIEAENPDFTFVEVNRDD----------------------YMEVAKKWDVYGIPSL 74
Cdd:COG0526    28 GKPVLvNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDEnpeavkaflkelglpypvlldpDGELAKAYGVRGIPTT 107

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1365260310  75 VVL-ENGQEIGRFVNreRKTKTQINEFLAQL 104
Cdd:COG0526   108 VLIdKDGKIVARHVG--PLSPEELEEALEKL 136

thioredoxin; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310   8 EELASFVKREGKIVFFFTAEWCGDCRFIKPFLPEIEAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQEIGRFV 87
Cdd:PTZ00051    9 AEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLL 88

thioredoxin-like protein

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1365260310  20 IVFFFTAEWCGDCRFIKPFLPeieaeNPDFTFVEVNRDDYMEVAKKWDVYGIPSLVvleNGQEIGRF 86
Cdd:PHA02125    1 MIYLFGAEWCANCKMVKPMLA-----NVEYTYVDVDTDEGVELTAKHHIRSLPTLV---NTSTLDRF 59

Thioredoxin;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310   2 IIPANIEELASFVKREGKIVFFfTAEWCGDCRFIKPFLPEIEAENPDFTFVEVNRDDYMEVAKKWDVYG---IPSLVVL- 77
Cdd:pfam14595  27 ELSEELIEKIKSIEKPLRILVI-TEDWCGDAAQNVPVLAKIAELNPNIELRILLRDENLELMDQYLTGGgraIPTFIFLd 105

                          90
                  ....*....|..
gi 1365260310  78 ENGQEIGRFVNR 89
Cdd:pfam14595 106 EDGEELGVWGPR 117

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 1365260310   8 EELASFVKrEGKIVFF-FTAEWCGDCRFIKPFL---PEI-EAENPDFTFVEV---NRDD----YMevaKKWDVYGIPSLV 75
Cdd:cd02953     2 AALAQALA-QGKPVFVdFTADWCVTCKVNEKVVfsdPEVqAALKKDVVLLRAdwtKNDPeitaLL---KRFGVFGPPTYL 77

                  ....*...
gi 1365260310  76 VLENGQEI 83
Cdd:cd02953    78 FYGPGGEP 85

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310  17 EGKIVF-FFTAEWCGDCRFIKP-F--LPEIEAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQEIGRFVNRERk 92
Cdd:cd02961    14 DSKDVLvEFYAPWCGHCKALAPeYekLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGSKEPVKYEGPR- 92

                  ....*....
gi 1365260310  93 TKTQINEFL 101
Cdd:cd02961    93 TLESLVEFI 101

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310  17 EGKIVF-FFTAEWCGDCRFIKP----FLPEIEAENPDFTFVEVNRD-------DYMEVAKKW------------------ 66
Cdd:cd02964    16 EGKTVGlYFSASWCPPCRAFTPklveFYEKLKEEGKNFEIVFVSRDrseesfnEYFSEMPPWlavpfedeelrellekqf 95

                          90       100
                  ....*....|....*....|
gi 1365260310  67 DVYGIPSLVVL-ENGQEIGR 85
Cdd:cd02964    96 KVEGIPTLVVLkPDGDVVTT 115

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310   7 IEELASFVKregkivffFTAEWCGDCRFIKPFLPEI----EAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQE 82
Cdd:cd03005    14 IAEGNHFVK--------FFAPWCGHCKRLAPTWEQLakkfNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEK 85

                  ....
gi 1365260310  83 IGRF 86
Cdd:cd03005    86 VDKY 89

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310  15 KREGKIVFF-FTAEWCGDCRFIKPFL---PEIEAE-NPDFTFVEV----NRDDYMEVAKKWDVYGIPSLVVL-ENGQEIG 84
Cdd:COG4232   317 RAEGKPVFVdFTADWCVTCKENERTVfsdPEVQAAlADDVVLLKAdvtdNDPEITALLKRFGRFGVPTYVFYdPDGEELP 396

                          90       100
                  ....*....|....*....|.
gi 1365260310  85 RFvnRERKTKTQINEFLAQLN 105
Cdd:COG4232   397 RL--GFMLTADEFLAALEKAK 415

disulphide isomerase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310   9 ELASFVKREGKIVFFFTAEWCGDCrfiKPFLPEIEA-------ENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQ 81
Cdd:PTZ00102   41 TFDKFITENEIVLVKFYAPWCGHC---KRLAPEYKKaakmlkeKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGN 117

                  ..
gi 1365260310  82 EI 83
Cdd:PTZ00102  118 PV 119

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1365260310  20 IVFFFTAEWCGDCRFIKPFLPEIEAE-NPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLEN 79
Cdd:cd02949    16 ILVLYTSPTCGPCRTLKPILNKVIDEfDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKD 76

Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1365260310   8 EELASFVKREGKIVFFFTAEWCGDCRFIKPFLPEIEAENPDFTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQEIGR 85
Cdd:cd02975    13 EEFFKEMKNPVDLVVFSSKEGCQYCEVTKQLLEELSELSDKLKLEIYDFDEDKEKAEKYGVERVPTTIFLQDGGKDGG 90

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 1365260310   4 PANIEELasfVKREGKIVFF-FTAEWCGDCrfiKPFLPEIE------AENPDFTFVEVNRDD-YMEVAKKWDVYGIPSL 74
Cdd:cd02998     7 DSNFDKV---VGDDKKDVLVeFYAPWCGHC---KNLAPEYEklaavfANEDDVVIAKVDADEaNKDLAKKYGVSGFPTL 79

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310  24 FTAEWCGDCRFIKPFLPE----IEAENPD---FTFVEVNRDDYMEVAKKWDVYGIPSLVVLENGQeigrFVNRERKTKTQ 96
Cdd:cd02996    25 FYADWCRFSQMLHPIFEEaaakIKEEFPDagkVVWGKVDCDKESDIADRYRINKYPTLKLFRNGM----MMKREYRGQRS 100

                  ....*
gi 1365260310  97 INEFL 101
Cdd:cd02996   101 VEALA 105

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260310  24 FTAEWCGDCRFIKPFLpeiEAENPDFTFVEVNRD--DYMEVAKKWDVYGIPSLVVleNGQEIGRFvnrerkTKTQINEFL 101
Cdd:COG0695     5 YTTPGCPYCARAKRLL---DEKGIPYEEIDVDEDpeAREELRERSGRRTVPVIFI--GGEHLGGF------DEGELDALL 73

                  .
gi 1365260310 102 A 102
Cdd:COG0695    74 A 74

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 1365260310  17 EGKIVF-FFTAEWCGDCRFIKPFLPEI------EAENPDFTFVEVNRD-----DYM-----------------EVAKKWD 67
Cdd:cd03009    17 EGKTVGlYFSASWCPPCRAFTPKLVEFyeklkeSGKNFEIVFISWDRDeesfnDYFskmpwlavpfsdrerrsRLNRTFK 96

                          90
                  ....*....|.
gi 1365260310  68 VYGIPSLVVLE 78
Cdd:cd03009    97 IEGIPTLIILD 107