ID   YRB1_YEAST              Reviewed;         201 AA.
AC   P41920; D6VRY9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 196.
DE   RecName: Full=Ran-specific GTPase-activating protein 1;
DE   AltName: Full=Chromosome stability protein 20;
DE   AltName: Full=Perinuclear array-localized protein;
DE   AltName: Full=Ran-binding protein 1;
DE            Short=RANBP1;
GN   Name=YRB1; Synonyms=CST20, HTN1, SFO1; OrderedLocusNames=YDR002W;
GN   ORFNames=YD8119.08;
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].
RC   STRAIN=H9;
RX   PubMed=7948031; DOI=10.1016/0167-4781(94)90233-x;
RA   Butler G., Wolfe K.H.;
RT   "Yeast homologue of mammalian Ran binding protein 1.";
RL   Biochim. Biophys. Acta 1219:711-712(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8444853; DOI=10.1016/s0021-9258(18)53463-3;
RA   Kopp M., Mueller H., Holzer H.;
RT   "Molecular analysis of the neutral trehalase gene from Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 268:4766-4774(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=7836422; DOI=10.1074/jbc.270.5.1975;
RA   Ouspenski I.I., Mueller U.W., Matynia A., Sazer S., Elledge S.J.,
RA   Brinkley B.R.;
RT   "Ran-binding protein-1 is an essential component of the Ran/RCC1 molecular
RT   switch system in budding yeast.";
RL   J. Biol. Chem. 270:1975-1978(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Trueheart J., Richards S., Macara I.G., Thorner J.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867; DOI=10.1038/387s075;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [6]
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   [7]
RP   CHARACTERIZATION.
RX   PubMed=7489726; DOI=10.1002/j.1460-2075.1995.tb00221.x;
RA   Schlenstedt G., Wong D.H., Koepp D.M., Silver P.A.;
RT   "Mutants in a yeast Ran binding protein are defective in nuclear
RT   transport.";
RL   EMBO J. 14:5367-5378(1995).
RN   [8]
RP   CHARACTERIZATION.
RX   PubMed=10825193; DOI=10.1128/mcb.20.12.4295-4308.2000;
RA   Kunzler M., Gerstberger T., Stutz F., Bischoff F.R., Hurt E.;
RT   "Yeast Ran-binding protein 1 (Yrb1) shuttles between the nucleus and
RT   cytoplasm and is exported from the nucleus via a CRM1 (XPO1)-dependent
RT   pathway.";
RL   Mol. Cell. Biol. 20:4295-4308(2000).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP   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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Important for the export of protein containing nuclear export
CC       signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1
CC       and GSP2.
CC   -!- SUBUNIT: Interacts with GSP1 and PRP20.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC       nucleus and cytoplasm.
CC   -!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}.
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DR   EMBL; Z33503; CAA83911.1; -; Genomic_DNA.
DR   EMBL; X65925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L38489; AAA57276.1; -; Genomic_DNA.
DR   EMBL; Z48008; CAA88062.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11849.1; -; Genomic_DNA.
DR   PIR; S50219; S50219.
DR   RefSeq; NP_010285.1; NM_001180310.1.
DR   PDB; 3M1I; X-ray; 2.00 A; B=11-201.
DR   PDB; 4GMX; X-ray; 2.10 A; B=62-201.
DR   PDB; 4GPT; X-ray; 2.22 A; B=62-201.
DR   PDB; 4HAT; X-ray; 1.78 A; B=62-201.
DR   PDB; 4HAU; X-ray; 2.00 A; B=62-201.
DR   PDB; 4HAV; X-ray; 2.00 A; B=62-201.
DR   PDB; 4HAW; X-ray; 1.90 A; B=62-201.
DR   PDB; 4HAX; X-ray; 2.28 A; B=62-201.
DR   PDB; 4HAY; X-ray; 2.30 A; B=62-201.
DR   PDB; 4HAZ; X-ray; 1.90 A; B=62-201.
DR   PDB; 4HB0; X-ray; 2.20 A; B=62-201.
DR   PDB; 4HB2; X-ray; 1.80 A; B=62-201.
DR   PDB; 4HB3; X-ray; 2.80 A; B=62-201.
DR   PDB; 4HB4; X-ray; 2.05 A; B=62-201.
DR   PDB; 4WVF; X-ray; 1.80 A; B=62-201.
DR   PDB; 5DH9; X-ray; 2.55 A; B=62-201.
DR   PDB; 5DHA; X-ray; 2.95 A; B=62-201.
DR   PDB; 5DHF; X-ray; 2.29 A; B=62-201.
DR   PDB; 5DI9; X-ray; 2.28 A; B=62-201.
DR   PDB; 5DIF; X-ray; 2.09 A; B=62-201.
DR   PDB; 5JLJ; X-ray; 2.50 A; B=62-201.
DR   PDB; 5UWH; X-ray; 2.26 A; B=62-201.
DR   PDB; 5UWI; X-ray; 2.14 A; B=62-201.
DR   PDB; 5UWJ; X-ray; 2.22 A; B=62-201.
DR   PDB; 5UWO; X-ray; 2.35 A; B=62-201.
DR   PDB; 5UWP; X-ray; 2.05 A; B=62-201.
DR   PDB; 5UWQ; X-ray; 2.28 A; B=62-201.
DR   PDB; 5UWR; X-ray; 2.24 A; B=62-201.
DR   PDB; 5UWS; X-ray; 2.40 A; B=62-201.
DR   PDB; 5UWT; X-ray; 2.34 A; B=62-201.
DR   PDB; 5UWU; X-ray; 2.24 A; B=62-201.
DR   PDB; 5UWW; X-ray; 2.15 A; B=62-201.
DR   PDB; 5YRO; X-ray; 2.40 A; B=62-201.
DR   PDB; 5YST; X-ray; 2.04 A; B=62-200.
DR   PDB; 5YSU; X-ray; 2.30 A; B=62-201.
DR   PDB; 5YTB; X-ray; 2.30 A; B=62-200.
DR   PDB; 5ZPU; X-ray; 2.60 A; B=62-201.
DR   PDB; 6A38; X-ray; 2.69 A; B=62-201.
DR   PDB; 6A3A; X-ray; 2.30 A; B=62-201.
DR   PDB; 6A3B; X-ray; 2.51 A; B=62-201.
DR   PDB; 6A3C; X-ray; 2.35 A; B=62-201.
DR   PDB; 6A3E; X-ray; 2.70 A; B=62-201.
DR   PDB; 6CIT; X-ray; 2.03 A; B=62-201.
DR   PDB; 6LQ9; X-ray; 2.50 A; B=62-201.
DR   PDB; 6M60; X-ray; 2.17 A; B=62-201.
DR   PDB; 6M6X; X-ray; 2.88 A; B=62-201.
DR   PDB; 6X2M; X-ray; 2.35 A; B=62-201.
DR   PDB; 6X2O; X-ray; 2.55 A; B=62-201.
DR   PDB; 6X2P; X-ray; 2.40 A; B=62-201.
DR   PDB; 6X2R; X-ray; 2.30 A; B=62-201.
DR   PDB; 6X2S; X-ray; 2.50 A; B=62-201.
DR   PDB; 6X2U; X-ray; 2.20 A; B=62-201.
DR   PDB; 6X2V; X-ray; 2.82 A; B=62-201.
DR   PDB; 6X2W; X-ray; 3.00 A; B=62-201.
DR   PDB; 6X2X; X-ray; 2.46 A; B=62-201.
DR   PDB; 6X2Y; X-ray; 2.30 A; B=62-201.
DR   PDB; 6XJP; X-ray; 2.80 A; B=62-201.
DR   PDB; 6XJR; X-ray; 1.94 A; B=62-201.
DR   PDB; 6XJS; X-ray; 1.94 A; B=62-201.
DR   PDB; 6XJT; X-ray; 2.41 A; B=62-201.
DR   PDB; 6XJU; X-ray; 2.19 A; B=62-201.
DR   PDB; 7CND; X-ray; 1.80 A; B=62-201.
DR   PDB; 7DBG; X-ray; 2.06 A; B=62-201.
DR   PDB; 7L5E; X-ray; 1.94 A; B=62-201.
DR   PDB; 7YPZ; X-ray; 2.15 A; B=62-201.
DR   PDB; 8HQ3; X-ray; 2.10 A; B=62-201.
DR   PDB; 8HQ4; X-ray; 2.12 A; B=62-201.
DR   PDB; 8HQ5; X-ray; 2.25 A; B=62-201.
DR   PDB; 8HQ6; X-ray; 2.03 A; B=62-201.
DR   PDB; 8HUF; X-ray; 2.29 A; B=62-201.
DR   PDB; 8HUG; X-ray; 2.15 A; B=62-201.
DR   PDB; 8ITV; X-ray; 2.30 A; B=62-201.
DR   PDB; 9OGN; X-ray; 2.41 A; B=62-201.
DR   PDB; 9OGO; X-ray; 2.37 A; B=62-201.
DR   PDB; 9VM1; X-ray; 2.45 A; B=62-201.
DR   AlphaFoldDB; P41920; -.
DR   MDRepo; P41920; -.
DR   SMR; P41920; -.
DR   BioGRID; 32055; 271.
DR   DIP; DIP-838N; -.
DR   FunCoup; P41920; 1225.
DR   IntAct; P41920; 8.
DR   MINT; P41920; -.
DR   STRING; 4932.YDR002W; -.
DR   iPTMnet; P41920; -.
DR   PaxDb; 4932-YDR002W; -.
DR   PeptideAtlas; P41920; -.
DR   EnsemblFungi; YDR002W_mRNA; YDR002W; YDR002W.
DR   GeneID; 851565; -.
DR   KEGG; sce:YDR002W; -.
DR   AGR; SGD:S000002409; -.
DR   SGD; S000002409; YRB1.
DR   VEuPathDB; FungiDB:YDR002W; -.
DR   eggNOG; KOG0864; Eukaryota.
DR   HOGENOM; CLU_067861_2_1_1; -.
DR   InParanoid; P41920; -.
DR   OMA; NFKDSFM; -.
DR   OrthoDB; 2357150at2759; -.
DR   BioCyc; YEAST:G3O-29624-MONOMER; -.
DR   BioGRID-ORCS; 851565; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P41920; -.
DR   PRO; PR:P41920; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P41920; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0051168; P:nuclear export; IBA:GO_Central.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR   GO; GO:0006405; P:RNA export from nucleus; IMP:SGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   CDD; cd13179; RanBD_RanBP1; 1.
DR   FunFam; 2.30.29.30:FF:000483; Ran-specific GTPase-activating protein 1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   IDEAL; IID50175; -.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000156; Ran_bind_dom.
DR   InterPro; IPR045255; RanBP1-like.
DR   InterPro; IPR045256; RanBP1_RanBD.
DR   PANTHER; PTHR23138:SF87; E3 SUMO-PROTEIN LIGASE RANBP2; 1.
DR   PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
DR   Pfam; PF00638; Ran_BP1; 1.
DR   SMART; SM00160; RanBD; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50196; RANBD1; 1.
DR   PDBsum; 3M1I; -.
DR   PDBsum; 4GMX; -.
DR   PDBsum; 4GPT; -.
DR   PDBsum; 4HAT; -.
DR   PDBsum; 4HAU; -.
DR   PDBsum; 4HAV; -.
DR   PDBsum; 4HAW; -.
DR   PDBsum; 4HAX; -.
DR   PDBsum; 4HAY; -.
DR   PDBsum; 4HAZ; -.
DR   PDBsum; 4HB0; -.
DR   PDBsum; 4HB2; -.
DR   PDBsum; 4HB3; -.
DR   PDBsum; 4HB4; -.
DR   PDBsum; 4WVF; -.
DR   PDBsum; 5DH9; -.
DR   PDBsum; 5DHA; -.
DR   PDBsum; 5DHF; -.
DR   PDBsum; 5DI9; -.
DR   PDBsum; 5DIF; -.
DR   PDBsum; 5JLJ; -.
DR   PDBsum; 5UWH; -.
DR   PDBsum; 5UWI; -.
DR   PDBsum; 5UWJ; -.
DR   PDBsum; 5UWO; -.
DR   PDBsum; 5UWP; -.
DR   PDBsum; 5UWQ; -.
DR   PDBsum; 5UWR; -.
DR   PDBsum; 5UWS; -.
DR   PDBsum; 5UWT; -.
DR   PDBsum; 5UWU; -.
DR   PDBsum; 5UWW; -.
DR   PDBsum; 5YRO; -.
DR   PDBsum; 5YST; -.
DR   PDBsum; 5YSU; -.
DR   PDBsum; 5YTB; -.
DR   PDBsum; 5ZPU; -.
DR   PDBsum; 6A38; -.
DR   PDBsum; 6A3A; -.
DR   PDBsum; 6A3B; -.
DR   PDBsum; 6A3C; -.
DR   PDBsum; 6A3E; -.
DR   PDBsum; 6CIT; -.
DR   PDBsum; 6LQ9; -.
DR   PDBsum; 6M60; -.
DR   PDBsum; 6M6X; -.
DR   PDBsum; 6X2M; -.
DR   PDBsum; 6X2O; -.
DR   PDBsum; 6X2P; -.
DR   PDBsum; 6X2R; -.
DR   PDBsum; 6X2S; -.
DR   PDBsum; 6X2U; -.
DR   PDBsum; 6X2V; -.
DR   PDBsum; 6X2W; -.
DR   PDBsum; 6X2X; -.
DR   PDBsum; 6X2Y; -.
DR   PDBsum; 6XJP; -.
DR   PDBsum; 6XJR; -.
DR   PDBsum; 6XJS; -.
DR   PDBsum; 6XJT; -.
DR   PDBsum; 6XJU; -.
DR   PDBsum; 7CND; -.
DR   PDBsum; 7DBG; -.
DR   PDBsum; 7L5E; -.
DR   PDBsum; 7YPZ; -.
DR   PDBsum; 8HQ3; -.
DR   PDBsum; 8HQ4; -.
DR   PDBsum; 8HQ5; -.
DR   PDBsum; 8HQ6; -.
DR   PDBsum; 8HUF; -.
DR   PDBsum; 8HUG; -.
DR   PDBsum; 8ITV; -.
DR   PDBsum; 9OGN; -.
DR   PDBsum; 9OGO; -.
DR   PDBsum; 9VM1; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; GTPase activation; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..201
FT                   /note="Ran-specific GTPase-activating protein 1"
FT                   /id="PRO_0000213670"
FT   DOMAIN          64..200
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   HELIX           64..68
FT                   /evidence="ECO:0007829|PDB:4HB2"
FT   STRAND          83..97
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   TURN            98..101
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   STRAND          102..116
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:5YST"
FT   STRAND          153..163
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:4WVF"
FT   STRAND          170..180
FT                   /evidence="ECO:0007829|PDB:4HAT"
FT   HELIX           181..199
FT                   /evidence="ECO:0007829|PDB:4HAT"
SQ   SEQUENCE   201 AA;  22953 MW;  46C3766B0906A75B CRC64;
     MSSEDKKPVV DKKEEAAPKP PSSAVFSMFG GKKAEKPETK KDEEDTKEET KKEGDDAPES
     PDIHFEPVVH LEKVDVKTME EDEEVLYKVR AKLFRFDADA KEWKERGTGD CKFLKNKKTN
     KVRILMRRDK TLKICANHII APEYTLKPNV GSDRSWVYAC TADIAEGEAE AFTFAIRFGS
     KENADKFKEE FEKAQEINKK A
//