Q6FNM5 (DOT1_CANGA) Reviewed, UniProtKB/Swiss-Prot

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
Short name=H3-K79-HMTase

Gene names

Name:	DOT1
Ordered Locus Names:	CAGL0J10516g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	652 AA.
Sequence status	Complete.
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 + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
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 methyltransferases, 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	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent 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 – 652	652	Histone-lysine N-methyltransferase, H3 lysine-79 specific		PRO_0000270607
Regions
	Region	467 – 469	3	S-adenosyl-L-methionine binding By similarity
	Region	529 – 530	2	S-adenosyl-L-methionine binding By similarity
	Motif	463 – 474	12	SAM-binding motif 1 By similarity
	Motif	544 – 553	10	SAM-binding motif 2 By similarity
Sites
	Binding site	445	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	492	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FNM5 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 2A94C532FB090699	FASTA	652	74,615
	10 20 30 40 50 60 MQEGLKLAER YNASLGSSQT YPIDNHHDKE SSTDVATDDI MEKDLHSGKT ISSQNSLDGS 70 80 90 100 110 120 EASTPVHQLE RPTIDVSERN DSRRKFRKKT SLDDLLDQAS KFQPQYEYSF PTSFLRKRKA 130 140 150 160 170 180 PQSNESDGEE EAKQNRTNKI VKQKKTKKNV KVTSKSKASV PIEEKHTINK QPKKTGTGGM 190 200 210 220 230 240 KRGPKPGRKK KSQKNTKNSI KKESTNAINN HKMYEMDSAS SRFAEHKNST NSESANNSFI 250 260 270 280 290 300 DWSLPKFSPP YQIFDIDNIN SYSNFQGQIY SSASLTKHHN EIGSKTPFSR NRDGSKSPID 310 320 330 340 350 360 DGQGKLIGLR SILYPDYYEE YLMDYKKVNF RYDGMAEIGK IMEYVGRIYL PEKYQKEYKE 370 380 390 400 410 420 TVVDIYNTAY DNKDLALSIS TVEKYNQFVG SIPKAEIVNH LAATKELPRS FLHDFLQIVY 430 440 450 460 470 480 TRSIHPYASK LKQYKAFSNY VYGELLPGFL TDVYSKCGLS KNHLFMDLGS GVGNCVIQAS 490 500 510 520 530 540 LEFGCRESFG CEIMEAASEL TEIQMREYSN RCKLFGFKQS KIDYSLRKSF INNEKVESLI 550 560 570 580 590 600 PECDVLLVNN FLFDGKLNYE VTKLLQKTKV GCKIISLKNI RASGYTLDTV NIESVLNRLE 610 620 630 640 650 VKKYRLDNNS VSWTHNGGEY FISTVLDRID ESLLDPQKRD RRNTHRPAKY TR

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: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380956 Genomic DNA. Translation: CAG61120.1.
RefSeq	XP_448169.1. XM_448169.1.
3D structure databases
HSSP	HSSP built from PDB template 1U2Z based on UniProtKB Q04089.
ProteinModelPortal	Q6FNM5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2889607.
GenomeReviews	Gene locus CAGL0J10516g in contig CR380956_GR.
KEGG	cgr:CAGL0J10516g.
Phylogenomic databases
eggNOG	fuNOG04919.
HOGENOM	HBG203300.
OMA	VYTRSIH.
OrthoDB	EOG412QDV.
Family and domain databases
InterPro	IPR013110. DOT1. IPR021162. Histone_H3-K79_MeTrfase. [Graphical view]
KO	K11427.
Pfam	PF08123. DOT1. 1 hit. [Graphical view]
PIRSF	PIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DOT1_CANGA

Accession

Primary (citable) accession number: Q6FNM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	July 19, 2004
Last modified:	December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program