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A5DNQ2 (A5DNQ2_PICGU) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | 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 RuleBase RU271113

EC=2.1.1.43 RuleBase RU271113
Alternative name(s):
Histone H3-K79 methyltransferase RuleBase RU271113
Gene names
ORF Names:PGUG_04903 EMBL EDK40806.2
OrganismMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome] EMBL EDK40806.2
Taxonomic identifier294746 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma

Protein attributes

Sequence length756 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. RuleBase RU271113

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. RuleBase RU271113

Enzyme regulation

Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3 By similarity. RuleBase RU271113

Subcellular location

Nucleus By similarity RuleBase RU271113.

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 By similarity. RuleBase RU271113

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family. RuleBase RU271113

Contains 1 DOT1 domain. RuleBase RU271113

Ontologies

Keywords
   Cellular componentNucleus RuleBase RU271113
   LigandS-adenosyl-L-methionine RuleBase RU271113
   Molecular functionChromatin regulator RuleBase RU271113
Methyltransferase RuleBase RU271113
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   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...

Sequences

Sequence LengthMass (Da)Tools
A5DNQ2 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 66B4EF1B62BEF45F

FASTA75686,139
        10         20         30         40         50         60 
MAQIQGVECG VFSNPPNGVG INTYVDMHHT IHKETPEPLT PSDTNSVMSI KSIVTPSQDL 

        70         80         90        100        110        120 
PEEKQPNGGI SIENKEDLVS ILKDLVQVDL SMTSLRTKID VIDGEKIQNI LNTLEEYDPE 

       130        140        150        160        170        180 
ATTVEERQSI EKLATSNHTL KEIRQEHPFR DDVAVDRLST EFNPFLRRIK FKNNLDRLLY 

       190        200        210        220        230        240 
ISQWYTSSEF NAGKKPDGEI EDEAPTDGRR LRPRRKTKQV SPEPEKIEEE KPRTKRRRTK 

       250        260        270        280        290        300 
ATVKDETPES KDSGDKYNPF DPENILEDTF LPLHGRHAFA DSIYIDAPSL PPLVTNVEPK 

       310        320        330        340        350        360 
LGVSVDTSAS NLITQHTKHY KNLPSSFPTL FITNSDGQEV ANVNNRIRIR FLLYPMHCEE 

       370        380        390        400        410        420 
YVLAQPKSNQ LDPVDEIIKF FQVNYGLYFS GSTKIRNIIV TNYCQKLREA VDDDDLASFV 

       430        440        450        460        470        480 
TIIDKWNQLV LHLSPNPSFW SDINPEIRMY TKKIEEKFSE SDLKINIFHT EIAKLVAKHQ 

       490        500        510        520        530        540 
GDKQDKNQTN ETNDNDHTVI PGSNGSVLAG DSISRYKRDF FCQLASNQKI SRYALHQILS 

       550        560        570        580        590        600 
RVYARVVSIS SNKLRYYKAF TAEVYGELLP CFTSEVLTKV GMKPHHKFYD LGSGVGNTTL 

       610        620        630        640        650        660 
QAALEFGAAL SGGCELMAHA SKLTLEQSNM VQRNLSVFGL KQLNLEWALS QSFADNEQVR 

       670        680        690        700        710        720 
RTVIDCDILI VNNYLFDAEL NYKVGKLLYG LRPGSKIVSL RNFISPRYKA SFDDTVFDYL 

       730        740        750 
QVEKHEMEHN MSVSWTANKV PYYISVVQKE VCKQYL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408160 Genomic DNA. Translation: EDK40806.2.
RefSeqXP_001482949.1. XM_001482899.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4929.A5DNQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5124947.
KEGGpgu:PGUG_04903.

Phylogenomic databases

KOK11427.
OrthoDBEOG7KH9VN.

Family and domain databases

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

Entry information

Entry nameA5DNQ2_PICGU
AccessionPrimary (citable) accession number: A5DNQ2
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: July 22, 2008
Last modified: April 16, 2014
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)