Reviewed, UniProtKB/Swiss-Prot Q1DKD8 (DOT1_COCIM)

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
ORF Names:	CIMG_09225

Organism

Coccidioides immitis (Valley fever fungus) [Complete proteome]

Taxonomic identifier

5501 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Coccidioides

Protein attributes

Sequence length	499 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 – 499	499	Histone-lysine N-methyltransferase, H3 lysine-79 specific		PRO_0000270609
Regions
	Region	330 – 332	3	S-adenosyl-L-methionine binding By similarity
	Region	390 – 391	2	S-adenosyl-L-methionine binding By similarity
	Motif	326 – 337	12	SAM-binding motif 1 By similarity
	Motif	405 – 414	10	SAM-binding motif 2 By similarity
Sites
	Binding site	308	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	354	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1DKD8-1 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: A436A6A833DC4099	FASTA	499	55,825
	10 20 30 40 50 60 MSFFDHLQKK GVGAIQAQKV QIRKVERKPS KVVSSSSSSS IAKPQRRLDT VSKPVAARRS 70 80 90 100 110 120 ASSASKPARH PQPRSRPPSR KRNTIEPTLF GSSEESDTDV SLDLRITKRA RVSSSVEPDL 130 140 150 160 170 180 HRRVRDTDAF SDGEAAFDMI HAADIISSKK SLGFNNAFGI EDGPIIVELQ YPGAPQKERY 190 200 210 220 230 240 QLVVPRDNDG FKPLDDIVQV LEIVSQNYIS EEHLALFEDE SNGLLRRLRR ALSNTSLTDF 250 260 270 280 290 300 LDGVKSYNET IQRLHQDGSI SRHLDSKHAL ALPLVERILT QVYSRTVSPR VDSLRQYENG 310 320 330 340 350 360 SDNVYGELLP RLVSKIFAET RLKSDQVFVD LGSGVGNVVL QAALEIGCES WGCEMMQNAC 370 380 390 400 410 420 DLAELQEKEF KTRCRLWGLQ PGQTHLKRGD FLEVDSVGKI LQKADVVLIN NQAFTPELNH 430 440 450 460 470 480 KLVNYFLDMK EGCQIVSLKS FVPAGHRIQS RNLNSPINLL SVKQKQYWSD SVSWTNAAGT 490 YFIATKDSSR LKAFLESST

References

[1]

"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives." Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W. Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH476730 Genomic DNA. Translation: EAS28021.1.
RefSeq	XP_001239604.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4558580.
Enzyme and pathway databases
BRENDA	2.1.1.43. 97654.
Family and domain databases
InterPro	IPR013110. DOT1. [Graphical view]
Pfam	PF08123. DOT1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DOT1_COCIM

Accession

Primary (citable) accession number: Q1DKD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	July 11, 2006
Last modified:	November 3, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)