Reviewed, UniProtKB/Swiss-Prot Q5A309 (DOT1_CANAL)

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:	CaO19.7402

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	1343 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
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 – 1343	1343	Histone-lysine N-methyltransferase, H3 lysine-79 specific		PRO_0000270606
Regions
	Region	1135 – 1137	3	S-adenosyl-L-methionine binding By similarity
	Region	1197 – 1198	2	S-adenosyl-L-methionine binding By similarity
	Motif	1131 – 1142	12	SAM-binding motif 1 By similarity
	Motif	1212 – 1221	10	SAM-binding motif 2 By similarity
Sites
	Binding site	1113	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	1160	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5A309-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: D4DE4546A3DD562C	FASTA	1,343	155,678
	10 20 30 40 50 60 MISGHLQTPD SSDHSGDEAK LTKPSGLESK TNELWSSDLE EELESRIMQP ATFSSILKQF 70 80 90 100 110 120 PSISEETIIS KIMSNKNCDK NNWKKKIYCY RYFLQPSKEE PDVGNMKSLV EKLEKLKLKK 130 140 150 160 170 180 WSASEIEQLF CNYLEDLTTS AVKVSIPGKT LDEVAAAVNN IHPRPRWTRK EIECLIKNEN 190 200 210 220 230 240 DFKKLEKDLF VRDLDSIKKK IRRDNLSIQN EIQDSEKKSP QSTDSNNKDS SRDLSRKERD 250 260 270 280 290 300 QLKKLLSKPI CFSELLAKFP GHSWEYIARE IIQLDSSEDN TIWLKKIYYY CVVYSISVDK 310 320 330 340 350 360 EITKYIGGGN RIYEKVRSDW SKIKTLDFFK DWSLQEFERL YCFAFHDLTK SALTKNFPSK 370 380 390 400 410 420 NLNDICKVVN ISFPKVPYTD REMKYLERHL DTPMQTLENN LPFRSRGSIH KKLEALKALT 430 440 450 460 470 480 ETTEQKQPPT KTRPKNEEEK NVENAAYMKE LIMFDLTLEA IENTFPSEPI EEIIKEIKNS 490 500 510 520 530 540 EIFDPLSFTR GEKELMAKLV KKGNLIDDCF DYFPLREEEF IRSKYAEAEY VSGRKMKFNT 550 560 570 580 590 600 PEERLAYEAK WTLFNMGKQE YGRGNRRSTK RYCEIDELSK LEQEASVKRS KKKIELTEEE 610 620 630 640 650 660 LEQRRKRSEH FRLCRLKKLE EKREKYRIEK AKRLEKIAAG LIKPSTSGYE LKDIVTSAEY 670 680 690 700 710 720 FQSIVGDKQK VQEGQKRKRI QTEYFAPEFI EKPKAVKLKT TKRQAEKNKI KKQLKREAQL 730 740 750 760 770 780 KIKKKKTIAP KKGKRRVKTN NGIIEEIKDV YKLSSEPYVE SEVEEEDEEE DYISPYDPPD 790 800 810 820 830 840 IISDSQVKLN GRHLYISSFY KELPEIPELK FVSLPHMEMS GNDITVAKQI MTTANDDILY 850 860 870 880 890 900 DDCLAYEIVA QHIKSYRDLP ISFPPVLDPI THELNSANIV RIRFFLYPEH YESFMLASPK 910 920 930 940 950 960 SNELDPVHEI AKLFMIQYSL YFSHSDTLKK IITEDYCHKL EHSVEENDFG EFMFVVDKWN 970 980 990 1000 1010 1020 QLVMKLSPNL ASVQNILGLK EDINEAPRAY LNQQEVSIPT NSDLKIETFY DEIMYESASP 1030 1040 1050 1060 1070 1080 LFNPINSNLE IDSESAPIPL GEVEIPNNVI EEINEKMPDN YIPDFFRRLK EKTEVSRYAM 1090 1100 1110 1120 1130 1140 QQILLRVYSR VVSTDSRKLR SYKAFTAETY GELLPSFTSE VLEKLNLLPT QKFYDLGSGV 1150 1160 1170 1180 1190 1200 GNTTFQAALE FGACSSGGCE IMEHASKLTE LQAGLIQKHL AVLGLQKLNL DFALHESFVG 1210 1220 1230 1240 1250 1260 NEKVRASCLD CDVLIINNYL FDGQLNDEVG KLLYGLRPGT KIVSLRNFIS PRYRATFDTV 1270 1280 1290 1300 1310 1320 FDFLSVEKHE MSDIMSVSWT ANKVPYYIST VEETIPREYL SREETKETSG KSKSVSPVGE 1330 1340 IENVAAAMMT PPTDSSESEI IKN

References

[1]

"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACQ01000074 Genomic DNA. Translation: EAK97059.1.
RefSeq	XP_716067.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3642236.
KEGG	cal:CaO19.7402.
Organism-specific databases
CGD	CAL0005423. orf19.7402.
Phylogenomic databases
OMA	NFISPRY.
Enzyme and pathway databases
BRENDA	2.1.1.43. 1124.
Family and domain databases
InterPro	IPR013110. DOT1. [Graphical view]
Pfam	PF08123. DOT1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DOT1_CANAL

Accession

Primary (citable) accession number: Q5A309

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	April 26, 2005
Last modified:	November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)