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B2AWA0 (B2AWA0_PODAN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 33. 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 PIRNR PIRNR017570
EC=2.1.1.43 PIRNR PIRNR017570
Alternative name(s):
Histone H3-K79 methyltransferase PIRNR PIRNR017570
OrganismPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) [Complete proteome]
Taxonomic identifier515849 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Lasiosphaeriaceae › Podospora ›

Protein attributes

Sequence length527 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

Sequences

Sequence LengthMass (Da)Tools
B2AWA0 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: D8294BDF1C4B5CC5

FASTA52759,069
        10         20         30         40         50         60 
MSIFNQKSKF KVKTEVRAVK KTLPEKPKPK PTSAPPSTSR IPSSVRASPS TTSTLRASPL 

        70         80         90        100        110        120 
PPSARKSQIG SSRYLDPSSA LKAPSSSTSS NSRKRPRASH SPASPSFDSD SDSDSASDDD 

       130        140        150        160        170        180 
WQDQLDPRKR LKRLEQLRRH DPNRRVRHPK MWKGDRESEG ELLPIIHAVE VASLSEKCQP 

       190        200        210        220        230        240 
VMGLSRDEVG VRLRYPGSNH REKYACSILM STFYNCHLLF STKVYELVKG KDKIEGAQDI 

       250        260        270        280        290        300 
LTVVRHVASI YLSEEEARPF LDQNSGIYRR LERCKNLNDG KGFKEALKEY SESLFALQRK 

       310        320        330        340        350        360 
GVIAKNLENM RGVPQELVAF ILDQVYDRTV APKVELLAKY ENGTDNVYGE LLHPFISDIF 

       370        380        390        400        410        420 
ERTQLTSDMV FVDLGSGVGN VVLQAALEIG CESWGCEMME NACNLADAQK REFAARCRLW 

       430        440        450        460        470        480 
GVAPGKVHLE RGDFRKNEPI LESLKRADVV LVNNQAFTSQ LNDNLVNMFL DLKIGCKIVS 

       490        500        510        520 
LKTFVHDNKL AENDVASSIL DVEHLTYPEE YVSWTGAAGT YCISTRK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633900 Genomic DNA. Translation: CAP68674.1.
RefSeqXP_001908001.1. XM_001907966.1.

3D structure databases

ProteinModelPortalB2AWA0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6192592.
KEGGpan:PODANSg5036.

Phylogenomic databases

KOK11427.

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 nameB2AWA0_PODAN
AccessionPrimary (citable) accession number: B2AWA0
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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