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Protein

Histone-lysine N-methyltransferase, H3 lysine-79 specific

Gene

DOT1

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

Enzyme regulationi

Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei492S-adenosyl-L-methioninePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
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 namesi
Name:DOT1
Ordered Locus Names:CAGL0J10516g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
Proteomesi
  • UP000002428 Componenti: Chromosome J

Organism-specific databases

CGDiCAL0133274. CAGL0J10516g.
EuPathDBiFungiDB:CAGL0J10516g.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002706071 – 652Histone-lysine N-methyltransferase, H3 lysine-79 specificAdd BLAST652

Interactioni

Protein-protein interaction databases

STRINGi284593.XP_448169.1.

Structurei

3D structure databases

ProteinModelPortaliQ6FNM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini321 – 638DOT1PROSITE-ProRule annotationAdd BLAST318

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni442 – 445S-adenosyl-L-methionine bindingPROSITE-ProRule annotation4
Regioni465 – 474S-adenosyl-L-methionine bindingPROSITE-ProRule annotation10
Regioni529 – 530S-adenosyl-L-methionine bindingPROSITE-ProRule annotation2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.PROSITE-ProRule annotation
Contains 1 DOT1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3924. Eukaryota.
ENOG410XSYC. LUCA.
HOGENOMiHOG000112251.
InParanoidiQ6FNM5.
KOiK11427.
OMAiGEYYIST.
OrthoDBiEOG092C18VU.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR021162. Dot1.
IPR025789. DOT1_dom.
IPR030445. H3-K79_meTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21451. PTHR21451. 1 hit.
PfamiPF08123. DOT1. 1 hit.
[Graphical view]
PIRSFiPIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51569. DOT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6FNM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQEGLKLAER YNASLGSSQT YPIDNHHDKE SSTDVATDDI MEKDLHSGKT
60 70 80 90 100
ISSQNSLDGS EASTPVHQLE RPTIDVSERN DSRRKFRKKT SLDDLLDQAS
110 120 130 140 150
KFQPQYEYSF PTSFLRKRKA PQSNESDGEE EAKQNRTNKI VKQKKTKKNV
160 170 180 190 200
KVTSKSKASV PIEEKHTINK QPKKTGTGGM KRGPKPGRKK KSQKNTKNSI
210 220 230 240 250
KKESTNAINN HKMYEMDSAS SRFAEHKNST NSESANNSFI DWSLPKFSPP
260 270 280 290 300
YQIFDIDNIN SYSNFQGQIY SSASLTKHHN EIGSKTPFSR NRDGSKSPID
310 320 330 340 350
DGQGKLIGLR SILYPDYYEE YLMDYKKVNF RYDGMAEIGK IMEYVGRIYL
360 370 380 390 400
PEKYQKEYKE TVVDIYNTAY DNKDLALSIS TVEKYNQFVG SIPKAEIVNH
410 420 430 440 450
LAATKELPRS FLHDFLQIVY TRSIHPYASK LKQYKAFSNY VYGELLPGFL
460 470 480 490 500
TDVYSKCGLS KNHLFMDLGS GVGNCVIQAS LEFGCRESFG CEIMEAASEL
510 520 530 540 550
TEIQMREYSN RCKLFGFKQS KIDYSLRKSF INNEKVESLI PECDVLLVNN
560 570 580 590 600
FLFDGKLNYE VTKLLQKTKV GCKIISLKNI RASGYTLDTV NIESVLNRLE
610 620 630 640 650
VKKYRLDNNS VSWTHNGGEY FISTVLDRID ESLLDPQKRD RRNTHRPAKY

TR
Length:652
Mass (Da):74,615
Last modified:July 19, 2004 - v1
Checksum:i2A94C532FB090699
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380956 Genomic DNA. Translation: CAG61120.1.
RefSeqiXP_448169.1. XM_448169.1.

Genome annotation databases

EnsemblFungiiCAG61120; CAG61120; CAGL0J10516g.
GeneIDi2889607.
KEGGicgr:CAGL0J10516g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380956 Genomic DNA. Translation: CAG61120.1.
RefSeqiXP_448169.1. XM_448169.1.

3D structure databases

ProteinModelPortaliQ6FNM5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284593.XP_448169.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG61120; CAG61120; CAGL0J10516g.
GeneIDi2889607.
KEGGicgr:CAGL0J10516g.

Organism-specific databases

CGDiCAL0133274. CAGL0J10516g.
EuPathDBiFungiDB:CAGL0J10516g.

Phylogenomic databases

eggNOGiKOG3924. Eukaryota.
ENOG410XSYC. LUCA.
HOGENOMiHOG000112251.
InParanoidiQ6FNM5.
KOiK11427.
OMAiGEYYIST.
OrthoDBiEOG092C18VU.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR021162. Dot1.
IPR025789. DOT1_dom.
IPR030445. H3-K79_meTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21451. PTHR21451. 1 hit.
PfamiPF08123. DOT1. 1 hit.
[Graphical view]
PIRSFiPIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51569. DOT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDOT1_CANGA
AccessioniPrimary (citable) accession number: Q6FNM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 19, 2004
Last modified: September 7, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.