ID   DOT1_USTMA              Reviewed;         798 AA.
AC   Q4P2W8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K79 methyltransferase;
DE   AltName: Full=H3-K79-HMTase;
GN   Name=DOT1; ORFNames=UM05545;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
CC   -!- FUNCTION: Histone methyltransferase that specifically methylates
CC       histone H3 to form H3K79me. This methylation is required for
CC       telomere silencing and for the pachytene checkpoint during the
CC       meiotic cell cycle by allowing the recruitment of RAD9 to double
CC       strand breaks. Nucleosomes are preferred as substrate compared to
CC       free histones (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone L-lysine =
CC       S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine.
CC   -!- ENZYME REGULATION: Ubiquitination of histone H2B to form
CC       H2BK123ub1 is required for efficient DOT1 methyltransferase
CC       activity on histone H3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- MISCELLANEOUS: In contrast to other lysine histone
CC       methyltransferase, it does not contain a SET domain, suggesting
CC       the existence of another mechanism for methylation of lysine
CC       residues of histones.
CC   -!- SIMILARITY: Belongs to the DOT1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AACP01000200; EAK86305.1; -; Genomic_DNA.
DR   RefSeq; XP_761692.1; -.
DR   GeneID; 3633676; -.
DR   KEGG; uma:UM05545.1; -.
DR   BRENDA; 2.1.1.43; 2320.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:EC.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR013110; DOT1.
DR   Pfam; PF08123; DOT1; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Complete proteome; Methyltransferase; Nucleus;
KW   Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    798       Histone-lysine N-methyltransferase, H3
FT                                lysine-79 specific.
FT                                /FTId=PRO_0000270616.
FT   MOTIF       577    588       SAM-binding motif 1 (By similarity).
FT   MOTIF       657    666       SAM-binding motif 2 (By similarity).
FT   BINDING     581    581       S-adenosyl-L-homocysteine (By
FT                                similarity).
FT   BINDING     605    605       S-adenosyl-L-homocysteine (By
FT                                similarity).
SQ   SEQUENCE   798 AA;  84989 MW;  F57A29F57EB14019 CRC64;
     MINFFGGKAP TAAQPASSTS TAVNGARFAS VSTSSSASAS AAGQPPLKKT KIAPSPVTVV
     TTVKKKVAPP TSVEPRDPIA ALSGYNSKNA LPEEKRRRII EERLAAQRQK SIESSLEAQL
     RAPTKSLSKS QSASSTSRRS AASFSKPKTK KPRKKVVDSD SDHDEFGDYG KSSRKPSTAP
     STPRASKRTS VDPHPTSDSY QKVGRDGVQP NYTVPRDIRA STSPTNTTAI PIDTQSRPSK
     PISSADIVTA NIKNYGPYFN GLGDAPRAVL EYPGTDASEE FLLLVPKDAD EYDPLMELLA
     TVRAIVTHYL TPEQRKAFGS LDSLEVSNNA GMILPSATHG ASASTSAVCN MVAALTDSNG
     INGARAKSAD LLDGQGSKAE RRNHLVGAGT YKDTGSMTPE PHANGISQTA PVSPTSQTSG
     ISASAGGSSV AKTVLVNNAL LRLDSPAPTE LSVASDHSST PAASCGTDPD SILRSFTKAR
     NRRDGPLFMR TLARFNSALA ALRDTGALAA NIADLGSCTG VPEGIWRLIQ DQVYARVVGP
     RVEELGRYQA FSDNVYGELL PRFMSEIAQL TLLGPEKVFV DLGSGVGNLL IQTSLQTGAE
     AYGCEMMRIP ASLASQQVVE AQLRWAAWGL RGGSAIEAWQ GDFGDHGGVR DVLKRADVVL
     VNNYAFLPKT NENLSLLFLD LPDGAKVVSL KPFVPPDFRL TQRTLSSPLA ILRVTERLYT
     SGCVSWADGG GKYYIQEVDR SLVREFLQNA GAATRAKRGK VSEGDDTVAA SDLMVGQDVR
     RKRWKAALQD DDEDDDEF
//