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Reviewed, UniProtKB/Swiss-Prot Q6FNM5 (DOT1_CANGA)

Last modified November 3, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Ordered Locus Names: CAGL0J10516g
OrganismCandida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier5478 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processchromatin 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 componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Histone-lysine N-methyltransferase, H3 lysine-79 specific
PRO_0000270607

Regions

Region467 – 4693S-adenosyl-L-methionine binding By similarity
Region529 – 5302S-adenosyl-L-methionine binding By similarity
Motif463 – 47412SAM-binding motif 1 By similarity
Motif544 – 55310SAM-binding motif 2 By similarity

Sites

Binding site4451S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4921S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FNM5-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 2A94C532FB090699

FASTA65274,615
        10         20         30         40         50         60 
MQEGLKLAER YNASLGSSQT YPIDNHHDKE SSTDVATDDI MEKDLHSGKT ISSQNSLDGS 

        70         80         90        100        110        120 
EASTPVHQLE RPTIDVSERN DSRRKFRKKT SLDDLLDQAS KFQPQYEYSF PTSFLRKRKA 

       130        140        150        160        170        180 
PQSNESDGEE EAKQNRTNKI VKQKKTKKNV KVTSKSKASV PIEEKHTINK QPKKTGTGGM 

       190        200        210        220        230        240 
KRGPKPGRKK KSQKNTKNSI KKESTNAINN HKMYEMDSAS SRFAEHKNST NSESANNSFI 

       250        260        270        280        290        300 
DWSLPKFSPP YQIFDIDNIN SYSNFQGQIY SSASLTKHHN EIGSKTPFSR NRDGSKSPID 

       310        320        330        340        350        360 
DGQGKLIGLR SILYPDYYEE YLMDYKKVNF RYDGMAEIGK IMEYVGRIYL PEKYQKEYKE 

       370        380        390        400        410        420 
TVVDIYNTAY DNKDLALSIS TVEKYNQFVG SIPKAEIVNH LAATKELPRS FLHDFLQIVY 

       430        440        450        460        470        480 
TRSIHPYASK LKQYKAFSNY VYGELLPGFL TDVYSKCGLS KNHLFMDLGS GVGNCVIQAS 

       490        500        510        520        530        540 
LEFGCRESFG CEIMEAASEL TEIQMREYSN RCKLFGFKQS KIDYSLRKSF INNEKVESLI 

       550        560        570        580        590        600 
PECDVLLVNN FLFDGKLNYE VTKLLQKTKV GCKIISLKNI RASGYTLDTV NIESVLNRLE 

       610        620        630        640        650 
VKKYRLDNNS VSWTHNGGEY FISTVLDRID ESLLDPQKRD RRNTHRPAKY TR 

« Hide

Cross-references

Sequence databases

CR380956 Genomic DNA. Translation: CAG61120.1.
RefSeqXP_448169.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FNM5.

Genome annotation databases

GeneID2889607.
GenomeReviewsGene locus CAGL0J10516g in contig CR380956_GR.
KEGGcgr:CAGL0J10516g.

Phylogenomic databases

HOGENOMQ6FNM5.
OMAYVYGELL.

Enzyme and pathway databases

BRENDA2.1.1.43. 189220.

Family and domain databases

InterProIPR013110. DOT1.
[Graphical view]
PfamPF08123. DOT1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDOT1_CANGA
AccessionPrimary (citable) accession number: Q6FNM5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 19, 2004
Last modified: November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents