Q5BH89 (DOT1_EMENI) 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:	AN0091

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	501 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 Reference 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 – 501	501	Histone-lysine N-methyltransferase, H3 lysine-79 specific		PRO_0000270612
Regions
	Region	332 – 334	3	S-adenosyl-L-methionine binding By similarity
	Region	392 – 393	2	S-adenosyl-L-methionine binding By similarity
	Motif	328 – 339	12	SAM-binding motif 1 By similarity
	Motif	407 – 416	10	SAM-binding motif 2 By similarity
Sites
	Binding site	310	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	356	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5BH89 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 0A6EF6F20A447F02	FASTA	501	56,359
	10 20 30 40 50 60 MGGFDYLQKG GTGFTLQVKK PQIRRVVQTR PAAPSPSANK ATPRTVPSGP QKKTPETASR 70 80 90 100 110 120 SVTGERGFSP SKRRLTPLRN RKRPTPEQRL SSDDDDDGSD TDTSLELRKR ARTGESAEPD 130 140 150 160 170 180 YGRRLRSLKA FSGDETRSLP IVHASEITSV QKPGKFKPAF ENMNQTSEIF LQYPSATPKE 190 200 210 220 230 240 RYEAVVPRDD DEFKPLDDIV QVIETVTQAY IPEDELDEFN NESTGIKRRL RRALARGSER 250 260 270 280 290 300 EFRESVKDYN VAIERLRRSG SIAKKLDATY RLSLPHVERI LTQIYSRTVS PRVDSLRQYE 310 320 330 340 350 360 NGTDNVYGEL LPRFISTIFK ETGLKSNHVF VDLGSGVGNV VLQAALEIGC ESWGCEMMQN 370 380 390 400 410 420 ACDLAELQQA EFKARCRLWG IAPGKTHLVR GDFLKEQSII DVLKRADVVL INNQAFTPQL 430 440 450 460 470 480 NNELINHFLD MKEGCQIVSL KSFVPVGHKI QSRNLNSPIN LLTVKQRQYW SNSVSWTDVG 490 500 GSYFIATKDS SRLKAFSESL A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACD01000003 Genomic DNA. Translation: EAA65269.1. BN001308 Genomic DNA. Translation: CBF90218.1.
RefSeq	XP_657695.1. XM_652603.1.
3D structure databases
HSSP	HSSP built from PDB template 1U2Z based on UniProtKB Q04089.
ProteinModelPortal	Q5BH89.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00002659; CADANIAP00002659; CADANIAG00002659.
GeneID	2875863.
KEGG	ani:AN0091.2.
Phylogenomic databases
OMA	IGCESWG.
OrthoDB	EOG412QDV.
PhylomeDB	Q5BH89.
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_EMENI

Accession

Primary (citable) accession number: Q5BH89
Secondary accession number(s): C8VQY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program