Reviewed, UniProtKB/Swiss-Prot Q4WVH4 (DOT1_ASPFU)

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:	AFUA_5G12110

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	502 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 – 502	502	Histone-lysine N-methyltransferase, H3 lysine-79 specific		PRO_0000270604
Regions
	Region	333 – 335	3	S-adenosyl-L-methionine binding By similarity
	Region	393 – 394	2	S-adenosyl-L-methionine binding By similarity
	Motif	329 – 340	12	SAM-binding motif 1 By similarity
	Motif	408 – 417	10	SAM-binding motif 2 By similarity
Sites
	Binding site	311	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	357	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WVH4-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 267DE547C9D276E4	FASTA	502	56,798
	10 20 30 40 50 60 MGFFDHLQKG GAFSLQAQKP QIRKVVQTRP PPPSRSSSHT PVRSLSQTSP PGRVKRPRDS 70 80 90 100 110 120 TSRSVSRDPD HRPSKRLSTP LRNRKRPTPE QRFSSDDDAS DTDTSFELRK RARTEDSAEP 130 140 150 160 170 180 DLARRIRSLK AFSEENVKPL PLVHAADITS KQKAGNFRRA FGGADRPTEI LLQYPSASLK 190 200 210 220 230 240 ERFNLVVPRD NDDFKPIDDI VHVIDIVSEN YIPESEADFF NNESTGIKRR LRRALAHSSE 250 260 270 280 290 300 TEFREAVASY NREIERLRRS GAIAKHLDAT HRLNLPLVER ILTQIYARTV SPRVESLRRY 310 320 330 340 350 360 ENGTDNVYGE LLPRFISTIF KETRLKSGHV FVDLGSGVGN VVLQAALEIG CESWGCEMMA 370 380 390 400 410 420 NACDLAELQQ TEFRARCRLW GIAPGKTNLV RGDFLQEQSI IDVLKRADVV LINNQAFTPQ 430 440 450 460 470 480 LNNEIINHFL DMKEGCQIVS LKSFVPAGHK IQSRNLYSPI NLLKVKQLNY WSNSVSWTDV 490 500 GGTYFIATKD SSRLKAFADS ME

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000003 Genomic DNA. Translation: EAL91402.1.
RefSeq	XP_753440.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q4WVH4.
Genome annotation databases
GeneID	3511508.
GenomeReviews	Gene locus dot1 in contig CM000173_GR.
KEGG	afm:AFUA_5G12110.
Phylogenomic databases
OMA	ESWGCEM.
Enzyme and pathway databases
BRENDA	2.1.1.43. 18841.
Family and domain databases
InterPro	IPR013110. DOT1. [Graphical view]
Pfam	PF08123. DOT1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DOT1_ASPFU

Accession

Primary (citable) accession number: Q4WVH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	July 5, 2005
Last modified:	November 3, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)