Reviewed, UniProtKB/Swiss-Prot Q6C4Y5 (DOT1_YARLI)

Names and origin

Protein names

Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-79 specific
    EC=2.1.1.43
Alternative name(s):
    Histone H3-K79 methyltransferase
    H3-K79-HMTase

Gene names

Name:	DOT1
Ordered Locus Names:	YALI0E22715g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

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.
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine.
Enzyme regulation	Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3 By similarity.
Subcellular location	Nucleus By similarity.
Miscellaneous	In contrast to other lysine histone methyltransferase, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Sequence similarities	Belongs to the DOT1 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Histone-lysine N-methyltransferase, H3 lysine-79 specific		PRO_0000270617
Regions
	Region	322 – 324	3	S-adenosyl-L-methionine binding By similarity
	Region	382 – 383	2	S-adenosyl-L-methionine binding By similarity
	Motif	318 – 329	12	SAM-binding motif 1 By similarity
	Motif	397 – 406	10	SAM-binding motif 2 By similarity
Sites
	Binding site	300	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	346	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6C4Y5-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 32609F4429A5D9F6	FASTA	492	53,624
	10 20 30 40 50 60 MFFSHLGKKN GGPTAKSSDV KRKVTKVKTR KPVVTSVSKS PSPSKTAPPP ATAAAAATAA 70 80 90 100 110 120 AKPSTPRKSR RKTPNIYQLS KSSLSEVDTE ESEREVSSSL STPGLYELVP RDIVTAGFGS 130 140 150 160 170 180 AELATSIHIT NASESGNLSM TDIYEPVSTD KSLSDRVKLG ALSCDFVEDY SLIKPKVPGE 190 200 210 220 230 240 FEPVREILSI MEMTALHFVD KGASEEIKHP VMDDCIMRRF RRSYEGGDLE GMKTSMKEFD 250 260 270 280 290 300 EVVKTQRAEG AILANLKQLT AVPQDLAYFL LNQVYSRIVS PESKSLRDYK AFSNNVYGEL 310 320 330 340 350 360 MPPFMSTVFQ KTDLQPSSVF VDLGSGVGNC TLQAALEVGC ESWGCEVMTN ASSLAEKQKI 370 380 390 400 410 420 ELYSRAKMFG IKTGDIHLVA SSFVHNDEVH SAISRADVLL VNNYAFDGTL NAHLLDMFLD 430 440 450 460 470 480 LKEGCKIVSL KSFVPVGHVI SEHNIESPVN ILKVQKLDFY SGSVSWTAAG GTYYISTVDR 490 SAIKAFLSKG GY

References

[1]

"Genome evolution in yeasts." 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. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382131 Genomic DNA. Translation: CAG79874.1.
RefSeq	XP_504277.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2912906.
GenomeReviews	Gene locus YALI0E22715g in contig CR382131_GR.
KEGG	yli:YALI0E22715g.
Enzyme and pathway databases
BRENDA	2.1.1.43. 3602.
Family and domain databases
InterPro	IPR013110. DOT1. [Graphical view]
Pfam	PF08123. DOT1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DOT1_YARLI

Accession

Primary (citable) accession number: Q6C4Y5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	August 16, 2004
Last modified:	September 22, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)