DOT1_YEAST
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 03-AUG-2022, entry version 187.
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 SMR; Q04089; -.
DR BioGRID; 32496; 309.
DR DIP; DIP-2560N; -.
DR IntAct; Q04089; 4.
DR MINT; Q04089; -.
DR STRING; 4932.YDR440W; -.
DR iPTMnet; Q04089; -.
DR MaxQB; Q04089; -.
DR PaxDb; Q04089; -.
DR PRIDE; Q04089; -.
DR EnsemblFungi; YDR440W_mRNA; YDR440W; YDR440W.
DR GeneID; 852050; -.
DR KEGG; sce:YDR440W; -.
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; WSDSVSW; -.
DR BioCyc; YEAST:G3O-29974-MON; -.
DR BRENDA; 2.1.1.360; 984.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
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 methyltransferase activity (H3-K79 specific); IDA:SGD.
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:0043486; P:histone exchange; IMP:SGD.
DR GO; GO:0034729; P:histone H3-K79 methylation; IDA:SGD.
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 assembly; 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:2000677; P:regulation of transcription regulatory region DNA binding; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 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; PTHR21451; 1.
DR Pfam; PF08123; DOT1; 1.
DR PIRSF; PIRSF017570; Histone_H3-K79_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 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
