ID   DOT1_GIBZE              Reviewed;         493 AA.
AC   Q4IJP1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=FG02567;
OS   Gibberella zeae (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella.
OX   NCBI_TaxID=5518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
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.
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DR   EMBL; AACM01000128; EAA68810.1; -; Genomic_DNA.
DR   RefSeq; XP_382743.1; -.
DR   GeneID; 2784179; -.
DR   KEGG; fgr:FG02567.1; -.
DR   BRENDA; 2.1.1.43; 74326.
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; Methyltransferase; Nucleus; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    493       Histone-lysine N-methyltransferase, H3
FT                                lysine-79 specific.
FT                                /FTId=PRO_0000270613.
FT   REGION      337    339       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      397    398       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   MOTIF       333    344       SAM-binding motif 1 (By similarity).
FT   MOTIF       412    421       SAM-binding motif 2 (By similarity).
FT   BINDING     314    314       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
FT   BINDING     361    361       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   493 AA;  55587 MW;  D41F5E293FF3475C CRC64;
     MRLFGGKNNK FKVDPPKIRI EKVVVDRPAQ KPKPKPNPAL SGSASRSSSS HHPSPKPLAR
     QASHSPYPSS CDEKRLERKR KAPSVSRKSP ASDRIEFDKD SDGEDDGWMT LDTKRQRKGT
     EDSGFVDPNR KLRSVRAFEE RMDSRKFIHA VDVASLEHKC VPVMGAQKDE VAIRLQYPSL
     QPREKYELVW GKDKIDAVEA SIKVVRHVAE TYLTEEEAEP FTNPNGGIIR RLEKASNRNI
     QDLMGFKAAL REYNEKLRAL VDDGVIAKNL DKMHELPQHL VAFILDQIYD RTVALKVELL
     SKYENGTDYV YGELLHPFIS KVLVEQTRMT SGQVFVDLGS GVGNVVLQAA LEIGCESWGC
     EMMENACNLA EEQKKEFDAR CMLWGVRPGK VHLERGDFRK NAPIHEALKR ADVVLVNNKA
     FTSQLNDDLV RMFLDLKSGC KVVSLKSFVA EKSNNHNIND VGSTILEVEE CIYPEGYVSW
     TNAGGSYFIS TRK
//