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A6QZ09 (A6QZ09_AJECN) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase, H3 lysine-79 specific PIRNR PIRNR017570

EC=2.1.1.43 PIRNR PIRNR017570
Alternative name(s):
Histone H3-K79 methyltransferase PIRNR PIRNR017570
Gene names
ORF Names:HCAG_02616 EMBL EDN06013.1
OrganismAjellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum) [Complete proteome] EMBL EDN06013.1
Taxonomic identifier339724 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces

Protein attributes

Sequence length504 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. PIRNR PIRNR017570

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. PIRNR PIRNR017570

Subcellular location

Nucleus By similarity PIRNR PIRNR017570.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family. PIRNR PIRNR017570

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region335 – 3384S-adenosyl-L-methionine binding By similarity PIRSR PIRSR017570-1
Region358 – 36710S-adenosyl-L-methionine binding By similarity PIRSR PIRSR017570-1
Region420 – 4212S-adenosyl-L-methionine binding By similarity PIRSR PIRSR017570-1

Sites

Binding site3841S-adenosyl-L-methionine By similarity PIRSR PIRSR017570-1

Sequences

Sequence LengthMass (Da)Tools
A6QZ09 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 62995B72D0105CB8

FASTA50456,224
        10         20         30         40         50         60 
MGFFDHLQTK GSIAIQPKRP QIRRVETATK PAQPTTSRAA PVASECSGPK PAPHSHQRRN 

        70         80         90        100        110        120 
RNPNPPTSSR RSSSSARASS TASDPTPSRH HDPAPRLKAR SLTRKRPSLI QRLTSSSDES 

       130        140        150        160        170        180 
DTEASFLEIR KRMKVSTSAE PDLQRQVRST VAFAEDAGKQ TIPIVHASDI ASMDKPAEFS 

       190        200        210        220        230        240 
RAFGDGSGSV SVEPFMVRLQ YPGISQGENY QLVIPREKEG FKPLDDIVHV VSIVSQHYIP 

       250        260        270        280        290        300 
EEHVHLFNDE TTGINRRFRR ALAHASESEF TAVVEEYNKI INRLRTDGII AKHLDNIHSL 

       310        320        330        340        350        360 
PLPLVERILT QTYSRTVSPR VESLRQYENG TDNVYGELLP RFISDIFKQT KLKSDQVFVD 

       370        380        390        400        410        420 
LGSGVGNVVL QAALEIGCES WGCEVMQNAC DVAELQGREF EARCRLWGLS PGIVRLIRGS 

       430        440        450        460        470        480 
FLTEESIIRA LHRADVVLIN NQAFTPQLNN EIINHFLDMK EGCQIVSLKS FVPAGHRIQA 

       490        500 
RNLNSPVNLL SVKQKNYWSG SFEA 

« Hide

References

[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NAm1 / WU24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476656 Genomic DNA. Translation: EDN06013.1.
RefSeqXP_001542445.1. XM_001542395.1.

3D structure databases

ProteinModelPortalA6QZ09.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5449222.
KEGGaje:HCAG_02616.

Phylogenomic databases

KOK11427.
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 nameA6QZ09_AJECN
AccessionPrimary (citable) accession number: A6QZ09
Entry history
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: April 16, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)