Q2U696 (DOT1_ASPOR) 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
ORF Names:	AO090120000327

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	335 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 – 335	335	Histone-lysine N-methyltransferase, H3 lysine-79 specific		PRO_0000270605
Regions
	Motif	162 – 173	12	SAM-binding motif 1 By similarity
	Motif	241 – 250	10	SAM-binding motif 2 By similarity
Sites
	Binding site	166	1	S-adenosyl-L-homocysteine By similarity
	Binding site	190	1	S-adenosyl-L-homocysteine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2U696 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 74C6EF0BCEFE1AFC	FASTA	335	38,178
	10 20 30 40 50 60 MVLARFANES TSYNRYNLVV PRDKDDFRPI DDIFQVIETV SQNYIPEDEA DYFDNESTGI 70 80 90 100 110 120 KRRLRRALAH ASEAEFRNVV TDYNEAIERL RRDGSIAQKL DSTHRLNLPL VERILTQIYS 130 140 150 160 170 180 RTVSPRVESL RQYENGTDNV YGELLPRFIS TIFKETGLKS GQVFVDLGSG VGNVVLQAAL 190 200 210 220 230 240 EIGCESWGCE MMQNACELAE LQQTEFRARC RLWGIAPGKT HLVRGDFLKE QSIIDVLKRA 250 260 270 280 290 300 DVILINNQAF TPQLNNELIN HFLDMKEGCQ IVSLKSFVPA AHKIQSRNLN SPINLLKVKQ 310 320 330 REYWSNSVSW TDVGGTYFIA TKDSSRLRAF AESMG

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007166 Genomic DNA. Translation: BAE62919.1.
3D structure databases
HSSP	HSSP built from PDB template 1U2Z based on UniProtKB Q04089.
ProteinModelPortal	Q2U696.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00011467; CADAORAP00011234; CADAORAG00011467.
GenomeReviews	Gene locus dot1 in contig AP007166_GR.
Phylogenomic databases
GeneTree	EFGT00050000004272.
OrthoDB	EOG412QDV.
Family and domain databases
InterPro	IPR013110. DOT1. IPR021162. Histone_H3-K79_MeTrfase. [Graphical view]
Pfam	PF08123. DOT1. 1 hit. [Graphical view]
PIRSF	PIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DOT1_ASPOR

Accession

Primary (citable) accession number: Q2U696

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program