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Reviewed, UniProtKB/Swiss-Prot Q756E1 (DOT1_ASHGO)

Last modified November 3, 2009. Version 48. 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: AER326C
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length575 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 – 575575Histone-lysine N-methyltransferase, H3 lysine-79 specific
PRO_0000270603

Regions

Region389 – 3913S-adenosyl-L-methionine binding By similarity
Region451 – 4522S-adenosyl-L-methionine binding By similarity
Motif385 – 39612SAM-binding motif 1 By similarity
Motif466 – 47510SAM-binding motif 2 By similarity

Sites

Binding site3671S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4141S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q756E1-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: ACE258C91ED8ED35

FASTA57563,831
        10         20         30         40         50         60 
MANNMNFVRV VANHNSQPSR HIYIKAPVTM AQTVRGADAA GNQNQNAGKG GVETTQLVGG 

        70         80         90        100        110        120 
QRPGAARKAN RMLLGLLEDS ARYDMKSDYS LQDTWLRKRR ATAQKTAKAE DKSVDTKKTR 

       130        140        150        160        170        180 
AAGKKTKPSE AGPDAKARSG MTSAPSSSST DAAAPAATGK ARNGKARAAS SVTRNTVLAN 

       190        200        210        220        230        240 
ASPFASPSED VIELQHQFFR ITDHQDCVNR EITSSLLLTP KDVADQQIVR LHFILYPDVS 

       250        260        270        280        290        300 
EEYKVTFGHP NNGVFNPIHE IGKCIKYAVE IYFPKTFKKK GSKLLQQLSK AYASMNQSAF 

       310        320        330        340        350        360 
VEAVEQYNDL VRAIPQDQVN EHLQQTKKIP RAFIHDILQM AYSRCVLPNV NGLKEYRSFS 

       370        380        390        400        410        420 
NFVYGELLPT FLSTVYQQCD LKPGQIFIDL GSGVGNCVVQ ASLEYGCALS FGCEIMKNAS 

       430        440        450        460        470        480 
ALAKSQLKEL EERCALWGVD LKPIEFSLRK SFIDNERVNE LLPQCDVLLI NNFIFDTKLN 

       490        500        510        520        530        540 
QAVEKLIQGL KPGCKIITLK NLRPSGYTIN FDDVENILNR LKVEKFTLPE DSVSWTYRGG 

       550        560        570 
GEYFISTVQA DIDESVFHSY AKGRVRGMRP AKYTK 

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

Cross-references

Sequence databases

AE016818 Genomic DNA. Translation: AAS53006.1.
RefSeqNP_985182.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ756E1.

Genome annotation databases

GeneID4621395.
GenomeReviewsGene locus AER326C in contig AE016818_GR.
KEGGago:AGOS_AER326C.
NMPDRfig|33169.1.peg.2827.

Organism-specific databases

AGDAER326C.

Phylogenomic databases

HOGENOMQ756E1.
OMALINNFIF.

Enzyme and pathway databases

BRENDA2.1.1.43. 279361.

Family and domain databases

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

Entry information

Entry nameDOT1_ASHGO
AccessionPrimary (citable) accession number: Q756E1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 48 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