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Reviewed, UniProtKB/Swiss-Prot Q2H9L1 (DOT1_CHAGB)

Last modified June 16, 2009. Version 23. 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
ORF Names: CHGG_03093
OrganismChaetomium globosum (Soil fungus) [Complete proteome]
Taxonomic identifier38033 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeChaetomium

Protein attributes

Sequence length510 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, DNA-dependent

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 – 510510Histone-lysine N-methyltransferase, H3 lysine-79 specific
PRO_0000270608

Regions

Region356 – 3583S-adenosyl-L-methionine binding By similarity
Region416 – 4172S-adenosyl-L-methionine binding By similarity
Motif352 – 36312SAM-binding motif 1 By similarity
Motif431 – 44010SAM-binding motif 2 By similarity

Sites

Binding site3341S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site3801S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2H9L1-1 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 1D678E4D39D6A9D4

FASTA51056,217
        10         20         30         40         50         60 
MSIFNQKSKF KVKTEVRKVK QAVEPTPESK KRYVGNGSAS ASTNGTPRAS PTPSSLQVKR 

        70         80         90        100        110        120 
PRPRPGAGAA SPATGPSLSS STSASPLDLT RKRRAPAGSS SSRSPATASP APRALSDSEP 

       130        140        150        160        170        180 
GSDDDDDDDW RDRLDPSKRR KRAHTEDPDR RLRHPRLWAG QGDEDKPGIV HAVQVASLAD 

       190        200        210        220        230        240 
KCQPVMKLAR DEVGVRLRYP GAKYTERYEL VWGKDKIDGA LDIMKVVKFV ASTYLTDAEA 

       250        260        270        280        290        300 
KPFLDHNLGI NRRLEKSKNT NDGEGFKAAL AEYNNQLLAL QTEGAIARNI DAMRGVPREL 

       310        320        330        340        350        360 
VEFILDQVYD RTVAPKVDLL AKYENGTDNV YGELLHPFIS DIFDRTKLSS DMVFVDLGSG 

       370        380        390        400        410        420 
VGNVTLQAAL ERGCESWGCE MMENACNLAE AQKKEFTARC RMWGIAPGKV HLERGDFRKS 

       430        440        450        460        470        480 
ERTLAALKRA DVVLVNNQAF TSELNDHLVN IFLDLKIGCK IVSLKTFVHD NKIAENDVAS 

       490        500        510 
SILEVEDLRY HEGYVSWTGA AGSFCISTRK 

« Hide

References

Cross-references

Sequence databases

CH408030 Genomic DNA. Translation: EAQ91158.1.
RefSeqXP_001229609.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4389504.

Enzyme and pathway databases

BRENDA2.1.1.43. 81575.

Family and domain databases

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

Entry information

Entry nameDOT1_CHAGB
AccessionPrimary (citable) accession number: Q2H9L1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: March 21, 2006
Last modified: June 16, 2009
This is version 23 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