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Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.43) (Histone H3-K79 methyltransferase) (H3-K79-HMTase)

 DOT1_CANGA              Reviewed;         652 AA.
Q6FNM5;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
12-SEP-2018, entry version 97.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific;
EC=2.1.1.43;
AltName: Full=Histone H3-K79 methyltransferase;
Short=H3-K79-HMTase;
Name=DOT1; OrderedLocusNames=CAGL0J10516g;
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
NRRL Y-65) (Yeast) (Torulopsis glabrata).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
Nakaseomyces/Candida clade.
NCBI_TaxID=284593;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Histone methyltransferase that specifically methylates
histone H3 to form H3K79me. This methylation is required for
telomere silencing and for the pachytene checkpoint during the
meiotic cell cycle by allowing the recruitment of RAD9 to double
strand breaks. Nucleosomes are preferred as substrate compared to
free histones (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00902}.
-!- ACTIVITY REGULATION: Ubiquitination of histone H2B to form
H2BK123ub1 is required for efficient DOT1 methyltransferase
activity on histone H3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- MISCELLANEOUS: In contrast to other lysine histone
methyltransferases, it does not contain a SET domain, suggesting
the existence of another mechanism for methylation of lysine
residues of histones.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. DOT1 family. {ECO:0000255|PROSITE-
ProRule:PRU00902}.
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EMBL; CR380956; CAG61120.1; -; Genomic_DNA.
RefSeq; XP_448169.1; XM_448169.1.
ProteinModelPortal; Q6FNM5; -.
SMR; Q6FNM5; -.
STRING; 284593.XP_448169.1; -.
PRIDE; Q6FNM5; -.
EnsemblFungi; CAG61120; CAG61120; CAGL0J10516g.
GeneID; 2889607; -.
KEGG; cgr:CAGL0J10516g; -.
CGD; CAL0133274; CAGL0J10516g.
EuPathDB; FungiDB:CAGL0J10516g; -.
eggNOG; KOG3924; Eukaryota.
eggNOG; ENOG410XSYC; LUCA.
HOGENOM; HOG000112251; -.
InParanoid; Q6FNM5; -.
KO; K11427; -.
OMA; YISTVME; -.
OrthoDB; EOG092C18VU; -.
Proteomes; UP000002428; Chromosome J.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IEA:InterPro.
GO; GO:0031493; F:nucleosomal histone binding; IEA:InterPro.
GO; GO:0006348; P:chromatin silencing at telomere; IEA:InterPro.
GO; GO:0000077; P:DNA damage checkpoint; IEA:InterPro.
GO; GO:0006281; P:DNA repair; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR021162; Dot1.
InterPro; IPR025789; DOT1_dom.
InterPro; IPR030445; H3-K79_meTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR21451; PTHR21451; 1.
Pfam; PF08123; DOT1; 1.
PIRSF; PIRSF017570; Histone_H3-K79_MeTrfase; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51569; DOT1; 1.
3: Inferred from homology;
Chromatin regulator; Complete proteome; Methyltransferase; Nucleus;
Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase.
CHAIN 1 652 Histone-lysine N-methyltransferase, H3
lysine-79 specific.
/FTId=PRO_0000270607.
DOMAIN 321 638 DOT1. {ECO:0000255|PROSITE-
ProRule:PRU00902}.
REGION 442 445 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00902}.
REGION 465 474 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00902}.
REGION 529 530 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00902}.
BINDING 492 492 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00902}.
SEQUENCE 652 AA; 74615 MW; 2A94C532FB090699 CRC64;
MQEGLKLAER YNASLGSSQT YPIDNHHDKE SSTDVATDDI MEKDLHSGKT ISSQNSLDGS
EASTPVHQLE RPTIDVSERN DSRRKFRKKT SLDDLLDQAS KFQPQYEYSF PTSFLRKRKA
PQSNESDGEE EAKQNRTNKI VKQKKTKKNV KVTSKSKASV PIEEKHTINK QPKKTGTGGM
KRGPKPGRKK KSQKNTKNSI KKESTNAINN HKMYEMDSAS SRFAEHKNST NSESANNSFI
DWSLPKFSPP YQIFDIDNIN SYSNFQGQIY SSASLTKHHN EIGSKTPFSR NRDGSKSPID
DGQGKLIGLR SILYPDYYEE YLMDYKKVNF RYDGMAEIGK IMEYVGRIYL PEKYQKEYKE
TVVDIYNTAY DNKDLALSIS TVEKYNQFVG SIPKAEIVNH LAATKELPRS FLHDFLQIVY
TRSIHPYASK LKQYKAFSNY VYGELLPGFL TDVYSKCGLS KNHLFMDLGS GVGNCVIQAS
LEFGCRESFG CEIMEAASEL TEIQMREYSN RCKLFGFKQS KIDYSLRKSF INNEKVESLI
PECDVLLVNN FLFDGKLNYE VTKLLQKTKV GCKIISLKNI RASGYTLDTV NIESVLNRLE
VKKYRLDNNS VSWTHNGGEY FISTVLDRID ESLLDPQKRD RRNTHRPAKY TR


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