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Q6CWV1 (DOT1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Short name=H3-K79-HMTase
Gene names
Name:DOT1
Ordered Locus Names:KLLA0B01287g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
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 + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

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 methyltransferases, 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 class I-like SAM-binding methyltransferase superfamily. DOT1 family.

Contains 1 DOT1 domain.

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_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Histone-lysine N-methyltransferase, H3 lysine-79 specific
PRO_0000270614

Regions

Domain245 – 558314DOT1
Region361 – 3644S-adenosyl-L-methionine binding By similarity
Region384 – 39310S-adenosyl-L-methionine binding By similarity
Region448 – 4492S-adenosyl-L-methionine binding By similarity

Sites

Binding site4111S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CWV1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: F830A57170781FF6

FASTA57264,796
        10         20         30         40         50         60 
MSTEATSSDA SVFSNMHSVD STRDNTRDNT RDNTPMNEGD TQGKRMTKST MALIEESMKY 

        70         80         90        100        110        120 
DMRSEYFLPM TFLRERRKPA RVESDEEDKL AEVKSKRRVS KKDQVKADIH STKIKKTGRP 

       130        140        150        160        170        180 
SNVKAGAKNT SKVTKQRSTK SQVSGKKRAR SISDGKVSSI DASRSLKASK KKHSSHADSL 

       190        200        210        220        230        240 
FLSNIEENVN PRPSFFNTTL IANPSSFTNK LTSSKMFVDD EEVTSLKGMK YILFPGVEEE 

       250        260        270        280        290        300 
YLICSKVQKF GYNPLPEIGQ SIESAVLLYF PNTYKTKGQE LVRSLNDAFE RSDDQSFEKI 

       310        320        330        340        350        360 
VLKYNDLIST IPRDLIVKNL SSNPDVPVSF VHFLLHTCYT RAIYPHARKL KKYTSFSNFV 

       370        380        390        400        410        420 
YGELMPDFLT IVFKKCGLNS NSIFMDLGSG VGNCVIQASL EFGCKLSFGC EIMDSASDMA 

       430        440        450        460        470        480 
ELQLKELKSR CDLWGINLPP IDFSLRKSFV DNERVRELIP QCDVILINNF IFDAPLNKEV 

       490        500        510        520        530        540 
EKVVQGLKAG SKIISLKSIR PPGYSINYDD MDNIFNRLHV ESFKLPENSV SWTYRSVGDY 

       550        560        570 
YISTVLDAID ESIFCPPILG RIRKKESIKY TR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382122 Genomic DNA. Translation: CAH01981.1.
RefSeqXP_451588.1. XM_451588.1.

3D structure databases

ProteinModelPortalQ6CWV1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.Q6CWV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2896923.
KEGGkla:KLLA0B01287g.

Phylogenomic databases

eggNOGNOG294902.
HOGENOMHOG000112251.
KOK11427.
OMANFVYGEL.
OrthoDBEOG7KH9VN.

Family and domain databases

InterProIPR013110. DOT1.
IPR025789. Histone_H3-K79_MeTrfase.
IPR021162. Histone_H3-K79_MeTrfase_fungi.
[Graphical view]
PfamPF08123. DOT1. 1 hit.
[Graphical view]
PIRSFPIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
PROSITEPS51569. DOT1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDOT1_KLULA
AccessionPrimary (citable) accession number: Q6CWV1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families