ID   DOT1_YEAST              Reviewed;         582 AA.
AC   Q04089; D6VT67;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific;
DE            EC=2.1.1.360 {ECO:0000269|PubMed:12080090, ECO:0000269|PubMed:12086673, ECO:0000269|PubMed:15292170};
DE   AltName: Full=Disrupter of telomere silencing protein 1;
DE   AltName: Full=Histone H3-K79 methyltransferase;
DE            Short=H3-K79-HMTase;
DE   AltName: Full=Lysine N-methyltransferase 4;
GN   Name=DOT1; Synonyms=KMT4, PCH1; OrderedLocusNames=YDR440W;
GN   ORFNames=D9461.26;
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=9755194; DOI=10.1093/genetics/150.2.613;
RA   Singer M.S., Kahana A., Wolf A.J., Meisinger L.L., Peterson S.E.,
RA   Goggin C., Mahowald M., Gottschling D.E.;
RT   "Identification of high-copy disruptors of telomeric silencing in
RT   Saccharomyces cerevisiae.";
RL   Genetics 150:613-632(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
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   [3]
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   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11029058; DOI=10.1091/mbc.11.10.3601;
RA   San-Segundo P.A., Roeder G.S.;
RT   "Role for the silencing protein Dot1 in meiotic checkpoint control.";
RL   Mol. Biol. Cell 11:3601-3615(2000).
RN   [5]
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-401.
RX   PubMed=12086673; DOI=10.1016/s0092-8674(02)00759-6;
RA   van Leeuwen F., Gafken P.R., Gottschling D.E.;
RT   "Dot1p modulates silencing in yeast by methylation of the nucleosome
RT   core.";
RL   Cell 109:745-756(2002).
RN   [6]
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-399 AND 401-GLY--GLY-403.
RX   PubMed=12080090; DOI=10.1101/gad.1001502;
RA   Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y.,
RA   Struhl K.;
RT   "Lysine methylation within the globular domain of histone H3 by Dot1 is
RT   important for telomeric silencing and Sir protein association.";
RL   Genes Dev. 16:1518-1527(2002).
RN   [7]
RP   FUNCTION.
RX   PubMed=12097318; DOI=10.1074/jbc.c200366200;
RA   Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.;
RT   "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3
RT   methyltransferase.";
RL   J. Biol. Chem. 277:30421-30424(2002).
RN   [8]
RP   ACTIVITY REGULATION.
RX   PubMed=12167634; DOI=10.1074/jbc.c200433200;
RA   Ng H.H., Xu R.-M., Zhang Y., Struhl K.;
RT   "Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-
RT   mediated methylation of histone H3 lysine 79.";
RL   J. Biol. Chem. 277:34655-34657(2002).
RN   [9]
RP   FUNCTION.
RX   PubMed=12152067; DOI=10.1038/nature00970;
RA   Briggs S.D., Xiao T., Sun Z.-W., Caldwell J.A., Shabanowitz J., Hunt D.F.,
RA   Allis C.D., Strahl B.D.;
RT   "Gene silencing: trans-histone regulatory pathway in chromatin.";
RL   Nature 418:498-498(2002).
RN   [10]
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   [11]
RP   FUNCTION.
RX   PubMed=12574507; DOI=10.1073/pnas.0437846100;
RA   Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.;
RT   "Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and
RT   mammalian cells: a potential mechanism for position-effect variegation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=15632126; DOI=10.1074/jbc.m414453200;
RA   Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.;
RT   "The DNA damage checkpoint response requires histone H2B ubiquitination by
RT   Rad6-Bre1 and H3 methylation by Dot1.";
RL   J. Biol. Chem. 280:9879-9886(2005).
RN   [13]
RP   FUNCTION.
RX   PubMed=16166626; DOI=10.1128/mcb.25.19.8430-8443.2005;
RA   Wysocki R., Javaheri A., Allard S., Sha F., Cote J., Kron S.J.;
RT   "Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage
RT   checkpoint functions of Rad9.";
RL   Mol. Cell. Biol. 25:8430-8443(2005).
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   IDENTIFICATION BY 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).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 158-582 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, DNA-BINDING, AND MUTAGENESIS OF
RP   ASP-301; TYR-350; TYR-372; GLU-374; GLU-422; TRP-543 AND TYR-550.
RX   PubMed=15292170; DOI=10.1074/jbc.m405902200;
RA   Sawada K., Yang Z., Horton J.R., Collins R.E., Zhang X., Cheng X.;
RT   "Structure of the conserved core of the yeast Dot1p, a nucleosomal histone
RT   H3 lysine 79 methyltransferase.";
RL   J. Biol. Chem. 279:43296-43306(2004).
CC   -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC       histone H3 to form H3K79me3. This methylation is required for telomere
CC       silencing and for the pachytene checkpoint during the meiotic cell
CC       cycle by allowing the recruitment of RAD9 to double strand breaks.
CC       Nucleosomes are preferred as substrate compared to free histones. Can
CC       bind to DNA (in vitro). {ECO:0000269|PubMed:11029058,
CC       ECO:0000269|PubMed:12097318, ECO:0000269|PubMed:12152067,
CC       ECO:0000269|PubMed:12574507, ECO:0000269|PubMed:15292170,
CC       ECO:0000269|PubMed:15632126, ECO:0000269|PubMed:16166626,
CC       ECO:0000269|PubMed:9755194}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA-
CC         COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00902,
CC         ECO:0000269|PubMed:12080090, ECO:0000269|PubMed:12086673,
CC         ECO:0000269|PubMed:15292170};
CC   -!- ACTIVITY REGULATION: Ubiquitination of histone H2B by the RAD6/UBC2-
CC       BRE1 complex to form H2BK123ub1 is required for efficient DOT1
CC       methyltransferase activity on histone H3. Interaction with DNA is
CC       required for optimal histone methyltransferase activity.
CC       {ECO:0000269|PubMed:12167634, ECO:0000269|PubMed:15292170}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8 to 9. {ECO:0000269|PubMed:15292170};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11029058}.
CC   -!- MISCELLANEOUS: In contrast to other lysine histone methyltransferases,
CC       it does not contain a SET domain, suggesting the existence of another
CC       mechanism for methylation of lysine residues of histones.
CC   -!- MISCELLANEOUS: Present with 2160 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. DOT1 family. {ECO:0000255|PROSITE-ProRule:PRU00902}.
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DR   EMBL; U33007; AAB64868.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12277.1; -; Genomic_DNA.
DR   PIR; S69720; S69720.
DR   RefSeq; NP_010728.1; NM_001180748.1.
DR   PDB; 1U2Z; X-ray; 2.20 A; A/B/C=158-582.
DR   PDB; 7K6P; EM; 3.20 A; K=176-580.
DR   PDB; 7K6Q; EM; 3.10 A; K=176-580.
DR   PDBsum; 1U2Z; -.
DR   PDBsum; 7K6P; -.
DR   PDBsum; 7K6Q; -.
DR   AlphaFoldDB; Q04089; -.
DR   EMDB; EMD-22691; -.
DR   EMDB; EMD-22692; -.
DR   SMR; Q04089; -.
DR   BioGRID; 32496; 310.
DR   DIP; DIP-2560N; -.
DR   IntAct; Q04089; 4.
DR   MINT; Q04089; -.
DR   STRING; 4932.YDR440W; -.
DR   iPTMnet; Q04089; -.
DR   MaxQB; Q04089; -.
DR   PaxDb; 4932-YDR440W; -.
DR   PeptideAtlas; Q04089; -.
DR   EnsemblFungi; YDR440W_mRNA; YDR440W; YDR440W.
DR   GeneID; 852050; -.
DR   KEGG; sce:YDR440W; -.
DR   AGR; SGD:S000002848; -.
DR   SGD; S000002848; DOT1.
DR   VEuPathDB; FungiDB:YDR440W; -.
DR   eggNOG; KOG3924; Eukaryota.
DR   GeneTree; ENSGT00390000013515; -.
DR   HOGENOM; CLU_027287_0_1_1; -.
DR   InParanoid; Q04089; -.
DR   OMA; KFKVDPP; -.
DR   OrthoDB; 146338at2759; -.
DR   BioCyc; YEAST:G3O-29974-MONOMER; -.
DR   BRENDA; 2.1.1.360; 984.
DR   BioGRID-ORCS; 852050; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q04089; -.
DR   PRO; PR:Q04089; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q04089; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0031151; F:histone H3K79 methyltransferase activity; IDA:SGD.
DR   GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0070911; P:global genome nucleotide-excision repair; IMP:SGD.
DR   GO; GO:0034729; P:histone H3-K79 methylation; IDA:MGI.
DR   GO; GO:0051598; P:meiotic recombination checkpoint signaling; IGI:SGD.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0031452; P:negative regulation of heterochromatin formation; IMP:SGD.
DR   GO; GO:0006334; P:nucleosome assembly; IDA:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR   GO; GO:0006301; P:postreplication repair; IGI:SGD.
DR   GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD.
DR   Gene3D; 1.10.260.170; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR021162; Dot1.
DR   InterPro; IPR025789; DOT1_dom.
DR   InterPro; IPR030445; H3-K79_meTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21451; HISTONE H3 METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR21451:SF0; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 1.
DR   Pfam; PF08123; DOT1; 1.
DR   PIRSF; PIRSF017570; Histone_H3-K79_MeTrfase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51569; DOT1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; DNA-binding; Methyltransferase; Nucleus;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..582
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-79
FT                   specific"
FT                   /id="PRO_0000186091"
FT   DOMAIN          254..568
FT                   /note="DOT1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..172
FT                   /note="Required for interaction with nucleosomes and DNA"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..143
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         372..375
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         395..404
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         422
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         459..460
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   MUTAGEN         301
FT                   /note="D->A,N: Abolishes methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         350
FT                   /note="Y->F: Reduces methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         372
FT                   /note="Y->F: Reduces methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         374
FT                   /note="E->A,Q: Abolishes methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         399
FT                   /note="G->R: Abolishes methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:12080090"
FT   MUTAGEN         401..403
FT                   /note="Missing: Abolishes methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:12080090"
FT   MUTAGEN         401
FT                   /note="G->A,R: Abolishes silencing function."
FT                   /evidence="ECO:0000269|PubMed:12086673"
FT   MUTAGEN         422
FT                   /note="E->A: Abolishes S-adenosyl-L-methionine binding and
FT                   methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         422
FT                   /note="E->D: No effect."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         543
FT                   /note="W->A: Abolishes methyltransferase activity, but not
FT                   S-adenosyl-L-methionine binding."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         550
FT                   /note="Y->A: Abolishes methyltransferase activity, but not
FT                   S-adenosyl-L-methionine binding."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   MUTAGEN         550
FT                   /note="Y->F: No effect."
FT                   /evidence="ECO:0000269|PubMed:15292170"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           196..201
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          248..252
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           264..277
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           293..301
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           305..319
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           324..331
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           340..353
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           355..361
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           368..370
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           377..386
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          394..399
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   TURN            401..403
FT                   /evidence="ECO:0007829|PDB:7K6Q"
FT   HELIX           404..413
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          416..422
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           425..444
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          452..458
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           464..469
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           470..472
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          474..478
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           485..495
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          503..508
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          519..521
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           525..528
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          529..535
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          541..543
FT                   /evidence="ECO:0007829|PDB:7K6P"
FT   STRAND          544..546
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   STRAND          549..555
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           561..563
FT                   /evidence="ECO:0007829|PDB:1U2Z"
FT   HELIX           566..569
FT                   /evidence="ECO:0007829|PDB:7K6Q"
SQ   SEQUENCE   582 AA;  66201 MW;  05CAA6A8F8CBAB9A CRC64;
     MGGQESISNN NSDSFIMSSP NLDSQESSIS PIDEKKGTDM QTKSLSSYSK GTLLSKQVQN
     LLEEANKYDP IYGSSLPRGF LRDRNTKGKD NGLVPLVEKV IPPIHKKTNN RNTRKKSSTT
     TKKDVKKPKA AKVKGKNGRT NHKHTPISKQ EIDTAREKKP LKKGRANKKN DRDSPSSTFV
     DWNGPCLRLQ YPLFDIEYLR SHEIYSGTPI QSISLRTNSP QPTSLTSDND TSSVTTAKLQ
     SILFSNYMEE YKVDFKRSTA IYNPMSEIGK LIEYSCLVFL PSPYAEQLKE TILPDLNASF
     DNSDTKGFVN AINLYNKMIR EIPRQRIIDH LETIDKIPRS FIHDFLHIVY TRSIHPQANK
     LKHYKAFSNY VYGELLPNFL SDVYQQCQLK KGDTFMDLGS GVGNCVVQAA LECGCALSFG
     CEIMDDASDL TILQYEELKK RCKLYGMRLN NVEFSLKKSF VDNNRVAELI PQCDVILVNN
     FLFDEDLNKK VEKILQTAKV GCKIISLKSL RSLTYQINFY NVENIFNRLK VQRYDLKEDS
     VSWTHSGGEY YISTVMEDVD ESLFSPAARG RRNRGTPVKY TR
//