ID URE2_YEAST Reviewed; 354 AA. AC P23202; D6W0W3; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=Transcriptional regulator URE2; DE AltName: Full=Disulfide reductase; DE EC=1.8.4.-; DE AltName: Full=Glutathione peroxidase; DE EC=1.11.1.9; GN Name=URE2; OrderedLocusNames=YNL229C; ORFNames=N1165; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=1990286; DOI=10.1128/mcb.11.2.822-832.1991; RA Coschigano P.W., Magasanik B.; RT "The URE2 gene product of Saccharomyces cerevisiae plays an important role RT in the cellular response to the nitrogen source and has homology to RT glutathione s-transferases."; RL Mol. Cell. Biol. 11:822-832(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 14085 / CBS 3093 / IFO 1997 / NRRL Y-12657, ATCC 9804 / RC CBS 400 / DSM 70478 / IFO 0210 / JCM 2220, Boots, CBS 2087, CBS 4734, RC CBS 5112, CBS 5287, CBS 7957, Chevalieri / ATCC 10604 / CBS 405 / IFO RC 0258 / NRRL Y-1546, Fleischmann, McPhie Sourdough, SAF, Sigma 1278B, RC Wyeast#1007, YJM 143, YJM 280, YJM 320, YJM 326, and YJM 415; RX PubMed=12177423; DOI=10.1073/pnas.162349599; RA Edskes H.K., Wickner R.B.; RT "Conservation of a portion of the S. cerevisiae Ure2p prion domain that RT interacts with the full-length protein."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16384-16391(2002). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8896273; RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s; RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.; RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open RT reading frames including a novel gene encoding a globin-like domain."; RL Yeast 12:1071-1076(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP PRION FORMATION. RX PubMed=7909170; DOI=10.1126/science.7909170; RA Wickner R.B.; RT "[URE3] as an altered URE2 protein: evidence for a prion analog in RT Saccharomyces cerevisiae."; RL Science 264:566-569(1994). RN [7] RP DOMAIN PRION. RX PubMed=7569955; DOI=10.1126/science.270.5233.93; RA Masison D.C., Wickner R.B.; RT "Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in RT prion-containing cells."; RL Science 270:93-95(1995). RN [8] RP FUNCTION. RX PubMed=8755910; DOI=10.1128/jb.178.15.4734-4736.1996; RA Blinder D., Coschigano P.W., Magasanik B.; RT "Interaction of the GATA factor Gln3p with the nitrogen regulator Ure2p in RT Saccharomyces cerevisiae."; RL J. Bacteriol. 178:4734-4736(1996). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10604478; DOI=10.1038/45287; RA Beck T., Hall M.N.; RT "The TOR signalling pathway controls nuclear localization of nutrient- RT regulated transcription factors."; RL Nature 402:689-692(1999). RN [10] RP FUNCTION. RX PubMed=10799523; DOI=10.1074/jbc.275.19.14408; RA Cunningham T.S., Andhare R., Cooper T.G.; RT "Nitrogen catabolite repression of DAL80 expression depends on the relative RT levels of Gat1p and Ure2p production in Saccharomyces cerevisiae."; RL J. Biol. Chem. 275:14408-14414(2000). RN [11] RP PRION FORMATION, AND PRION CURING. RX PubMed=11073991; DOI=10.1128/mcb.20.23.8916-8922.2000; RA Moriyama H., Edskes H.K., Wickner R.B.; RT "[URE3] prion propagation in Saccharomyces cerevisiae: requirement for RT chaperone Hsp104 and curing by overexpressed chaperone Ydj1p."; RL Mol. Cell. Biol. 20:8916-8922(2000). RN [12] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [13] RP FUNCTION. RX PubMed=15371425; DOI=10.1074/jbc.m406612200; RA Bai M., Zhou J.M., Perrett S.; RT "The yeast prion protein Ure2 shows glutathione peroxidase activity in both RT native and fibrillar forms."; RL J. Biol. Chem. 279:50025-50030(2004). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF ALA-122 AND ASN-124. RX PubMed=19321443; DOI=10.1074/jbc.m901189200; RA Zhang Z.R., Perrett S.; RT "Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a RT native-like dimer within fibrils."; RL J. Biol. Chem. 284:14058-14067(2009). RN [16] RP INTERACTION WITH NNK1. RX PubMed=20489023; DOI=10.1126/science.1176495; RA Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B., RA Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D., RA Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C., RA Nesvizhskii A.I., Tyers M.; RT "A global protein kinase and phosphatase interaction network in yeast."; RL Science 328:1043-1046(2010). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 95-354 IN COMPLEX WITH RP GLUTATHIONE AND INHIBITORS. RX PubMed=11695904; DOI=10.1021/bi011007b; RA Bousset L., Belrhali H., Melki R., Morera S.; RT "Crystal structures of the yeast prion Ure2p functional region in complex RT with glutathione and related compounds."; RL Biochemistry 40:13564-13573(2001). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 97-354. RX PubMed=11171973; DOI=10.1073/pnas.98.4.1459; RA Umland T.C., Taylor K.L., Rhee S., Wickner R.B., Davies D.R.; RT "The crystal structure of the nitrogen regulation fragment of the yeast RT prion protein Ure2p."; RL Proc. Natl. Acad. Sci. U.S.A. 98:1459-1464(2001). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-353. RX PubMed=11342133; DOI=10.1016/s0969-2126(00)00553-0; RA Bousset L., Belrhali H., Janin J., Melki R., Morera S.; RT "Structure of the globular region of the prion protein Ure2 from the yeast RT Saccharomyces cerevisiae."; RL Structure 9:39-46(2001). RN [21] RP STRUCTURE BY NMR OF 10-39. RX PubMed=16060675; DOI=10.1021/bi050724t; RA Chan J.C., Oyler N.A., Yau W.M., Tycko R.; RT "Parallel beta-sheets and polar zippers in amyloid fibrils formed by RT residues 10-39 of the yeast prion protein Ure2p."; RL Biochemistry 44:10669-10680(2005). RN [22] RP STRUCTURE BY NMR OF 1-89, AND DOMAIN PRION. RX PubMed=17953455; DOI=10.1021/bi700826b; RA Baxa U., Wickner R.B., Steven A.C., Anderson D.E., Marekov L.N., Yau W.M., RA Tycko R.; RT "Characterization of beta-sheet structure in Ure2p(1-89) yeast prion RT fibrils by solid-state nuclear magnetic resonance."; RL Biochemistry 46:13149-13162(2007). CC -!- FUNCTION: Plays an important role in nitrogen catabolite repression. CC Down-regulates the expression of many genes involved in nitrogen CC utilization by inhibiting the GATA transcriptional activators GLN3 and CC GAT1. Under good nitrogen conditions, binds to the phosphorylated forms CC of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing CC transcription of genes expressed upon nitrogen limitation. Is also an CC atypical glutaredoxin without a catalytical cysteine residue. Has CC glutathione peroxidase and thiol:disulfide oxidoreductase activities in CC both native and fibrillar form. Also shows insulin disulfide reductase CC and dehydroascorbic acid reductase (DHAR) activities. CC {ECO:0000269|PubMed:10604478, ECO:0000269|PubMed:10799523, CC ECO:0000269|PubMed:15371425, ECO:0000269|PubMed:19321443, CC ECO:0000269|PubMed:1990286, ECO:0000269|PubMed:8755910}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; CC Evidence={ECO:0000269|PubMed:19321443}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.4 mM for bis-(2-hydroxyethyl) disulfide (HEDS) CC {ECO:0000269|PubMed:19321443}; CC Note=kcat is 1.2 sec(-1) with bis-(2-hydroxyethyl) disulfide (HEDS) CC as substrate.; CC -!- SUBUNIT: Homodimer. Interacts with NNK1. {ECO:0000269|PubMed:11695904, CC ECO:0000269|PubMed:20489023}. CC -!- INTERACTION: CC P23202; P18494: GLN3; NbExp=2; IntAct=EBI-20138, EBI-7657; CC P23202; P36003: NNK1; NbExp=4; IntAct=EBI-20138, EBI-9796; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10604478}. CC -!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is CC unstructured in its native, soluble form, and which forms a parallel CC in-register beta-sheet in its amyloid form. CC {ECO:0000269|PubMed:17953455, ECO:0000269|PubMed:7569955}. CC -!- MISCELLANEOUS: [URE3] is the prion form of URE2. [URE3] is the result CC of a conformational change of the cellular URE2 protein that becomes CC self-propagating and infectious. This conformational change generates a CC form of URE2 that assembles into amyloid fibrils. [URE3]-aggregates CC sequester soluble URE2, which then fails to retain GLN3 in the CC cytoplasm, resulting in GLN3 activation and consequently derepression CC of genes that are required for utilization of poor nirogen sources CC (PubMed:7909170). [URE3] can be cured by GdnHCl and by deletion of the CC molecular chaperone HSP104, which is required for [URE3] propagation CC (PubMed:11073991). {ECO:0000305|PubMed:11073991, CC ECO:0000305|PubMed:7909170}. CC -!- MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Mad yeast disease - Issue 47 CC of June 2004; CC URL="https://web.expasy.org/spotlight/back_issues/047"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35268; AAA35201.1; -; Genomic_DNA. DR EMBL; AF525174; AAM93167.1; -; Genomic_DNA. DR EMBL; AF525175; AAM93168.1; -; Genomic_DNA. DR EMBL; AF525176; AAM93169.1; -; Genomic_DNA. DR EMBL; AF525177; AAM93170.1; -; Genomic_DNA. DR EMBL; AF525178; AAM93171.1; -; Genomic_DNA. DR EMBL; AF525179; AAM93172.1; -; Genomic_DNA. DR EMBL; AF525180; AAM93173.1; -; Genomic_DNA. DR EMBL; AF525181; AAM93174.1; -; Genomic_DNA. DR EMBL; AF525182; AAM93175.1; -; Genomic_DNA. DR EMBL; AF525183; AAM93176.1; -; Genomic_DNA. DR EMBL; AF525184; AAM93177.1; -; Genomic_DNA. DR EMBL; AF525185; AAM93178.1; -; Genomic_DNA. DR EMBL; AF525186; AAM93179.1; -; Genomic_DNA. DR EMBL; AF525187; AAM93180.1; -; Genomic_DNA. DR EMBL; AF525188; AAM93181.1; -; Genomic_DNA. DR EMBL; AF525189; AAM93182.1; -; Genomic_DNA. DR EMBL; AF525190; AAM93183.1; -; Genomic_DNA. DR EMBL; AF525191; AAM93184.1; -; Genomic_DNA. DR EMBL; AF525192; AAM93185.1; -; Genomic_DNA. DR EMBL; Z69381; CAA93369.1; -; Genomic_DNA. DR EMBL; Z71505; CAA96134.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10329.1; -; Genomic_DNA. DR PIR; A39609; A39609. DR RefSeq; NP_014170.1; NM_001183067.1. DR PDB; 1G6W; X-ray; 2.50 A; A/B/C/D=94-354. DR PDB; 1G6Y; X-ray; 2.80 A; A/B=94-354. DR PDB; 1HQO; X-ray; 2.30 A; A/B=97-354. DR PDB; 1JZR; X-ray; 2.90 A; A/B/C/D=95-354. DR PDB; 1K0A; X-ray; 2.50 A; A/B=95-354. DR PDB; 1K0B; X-ray; 2.50 A; A/B/C/D=95-354. DR PDB; 1K0C; X-ray; 2.50 A; A/B/C/D=95-354. DR PDB; 1K0D; X-ray; 2.20 A; A/B/C/D=95-354. DR PDBsum; 1G6W; -. DR PDBsum; 1G6Y; -. DR PDBsum; 1HQO; -. DR PDBsum; 1JZR; -. DR PDBsum; 1K0A; -. DR PDBsum; 1K0B; -. DR PDBsum; 1K0C; -. DR PDBsum; 1K0D; -. DR AlphaFoldDB; P23202; -. DR BMRB; P23202; -. DR SMR; P23202; -. DR BioGRID; 35609; 369. DR DIP; DIP-1308N; -. DR IntAct; P23202; 33. DR MINT; P23202; -. DR STRING; 4932.YNL229C; -. DR MoonProt; P23202; -. DR iPTMnet; P23202; -. DR MaxQB; P23202; -. DR PaxDb; 4932-YNL229C; -. DR PeptideAtlas; P23202; -. DR EnsemblFungi; YNL229C_mRNA; YNL229C; YNL229C. DR GeneID; 855492; -. DR KEGG; sce:YNL229C; -. DR AGR; SGD:S000005173; -. DR SGD; S000005173; URE2. DR VEuPathDB; FungiDB:YNL229C; -. DR eggNOG; KOG0867; Eukaryota. DR HOGENOM; CLU_011226_14_1_1; -. DR InParanoid; P23202; -. DR OMA; KFFQNQP; -. DR OrthoDB; 1404190at2759; -. DR BioCyc; YEAST:YNL229C-MONOMER; -. DR BioGRID-ORCS; 855492; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P23202; -. DR PRO; PR:P23202; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P23202; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD. DR GO; GO:0051219; F:phosphoprotein binding; IDA:SGD. DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro. DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IMP:SGD. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0032447; P:protein urmylation; IMP:SGD. DR GO; GO:0006808; P:regulation of nitrogen utilization; IMP:SGD. DR CDD; cd10293; GST_C_Ure2p; 1. DR CDD; cd03048; GST_N_Ure2p_like; 1. DR DisProt; DP00353; -. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017298; Ure2. DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1. DR PANTHER; PTHR44051:SF3; TRANSCRIPTIONAL REGULATOR URE2; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR PIRSF; PIRSF037861; Prion_URE2; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG00358; Main_(cytGST); 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Amyloid; Cytoplasm; Nitrate assimilation; KW Oxidoreductase; Prion; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..354 FT /note="Transcriptional regulator URE2" FT /id="PRO_0000186013" FT DOMAIN 112..196 FT /note="GST N-terminal" FT DOMAIN 205..354 FT /note="GST C-terminal" FT REGION 2..89 FT /note="Prion domain (PrD)" FT REGION 22..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 124 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:11695904" FT BINDING 151 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:11695904" FT BINDING 164..165 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT BINDING 180..181 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT MOD_RES 2 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MUTAGEN 122 FT /note="A->S: Reduces glutaredoxin activity." FT /evidence="ECO:0000269|PubMed:19321443" FT MUTAGEN 124 FT /note="N->A,V: Abolishes glutaredoxin activity." FT /evidence="ECO:0000269|PubMed:19321443" FT MUTAGEN 313 FT /note="F->S: Destroys protein function." FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:1K0D" FT STRAND 111..118 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 123..134 FT /evidence="ECO:0007829|PDB:1K0D" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:1K0D" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 154..157 FT /evidence="ECO:0007829|PDB:1K0D" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:1K0D" FT TURN 171..175 FT /evidence="ECO:0007829|PDB:1K0D" FT STRAND 176..180 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 181..196 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 206..222 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 224..235 FT /evidence="ECO:0007829|PDB:1K0D" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:1G6W" FT HELIX 242..271 FT /evidence="ECO:0007829|PDB:1K0D" FT TURN 276..278 FT /evidence="ECO:0007829|PDB:1K0B" FT HELIX 279..284 FT /evidence="ECO:0007829|PDB:1G6W" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:1G6W" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:1G6W" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:1G6W" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 314..317 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 320..323 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 327..330 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 332..342 FT /evidence="ECO:0007829|PDB:1K0D" FT HELIX 345..350 FT /evidence="ECO:0007829|PDB:1K0D" SQ SEQUENCE 354 AA; 40271 MW; 2C628976034B0F1C CRC64; MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN SSSNNNNVQN NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS RITKFFQEQP LEGYTLFSHR SAPNGFKVAI VLSELGFHYN TIFLDFNLGE HRAPEFVSVN PNARVPALID HGMDNLSIWE SGAILLHLVN KYYKETGNPL LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK IASAVERYTD EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA LRGE //