A2QTN4 (A2QTN4_ASPNC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended 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:

An09g02720 EMBL CAK40209.1

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Protein existence	Inferred 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

Ontologies

Keywords
Biological process	Transcription Transcription regulation PIRNR PIRNR017570
Cellular component	Nucleus PIRNR PIRNR017570
Ligand	S-adenosyl-L-methionine PIRNR PIRNR017570
Molecular function	Chromatin regulator PIRNR PIRNR017570 Methyltransferase PIRNR PIRNR017570 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	histone lysine methylation Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A2QTN4 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 377590381809B001	FASTA	500	55,943
	10 20 30 40 50 60 MGFFDHLQKG GAFSLQPKKP QIRKVVQTRT APASRSTSQT PGPSSRTPPA QLKAQQSASR 70 80 90 100 110 120 SVSRDRDPPS AKRRHGTPAQ SRKRQTPELR LSSDDDASDT DSSFEVRKRA RTGDSAEPDP 130 140 150 160 170 180 ARRVRSLKAF SEDSVRSLPM IHAADITSRQ KAGNFKPAFG AAKPLPELLL QYLSTSAPER 190 200 210 220 230 240 YNLVVPRDHD DFKPIDDIVQ VLDIVSQNYI PDEAADEFNN ESTGIKRRLR RALAHLSEAD 250 260 270 280 290 300 FRSVVNEYNE AIVRLRRDGS IAKKLDSTSR LNLPHVERIL NQIYSRTVSP RVESLRQYEN 310 320 330 340 350 360 GTDNVYGELL PRFISTIFKE TGLKSGQVFV DLGSGVGNVV LQAALEIGCE SWGCEMMDNA 370 380 390 400 410 420 CDLADLQQAE FRSRCRLWGI APGKTHLVRG DFLKEQPIID VLKRADVILI NNQAFTPQLN 430 440 450 460 470 480 NELINHFLDM KEGCQIVSLK SFVPAGHKIQ SRNLNSPINL LKVKQRNYWS NSVSWTDVGG 490 500 TYFIATKDSS RLKAFVDSMQ

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270196 Genomic DNA. Translation: CAK40209.1.
RefSeq	XP_001393586.1. XM_001393549.2.
3D structure databases
ProteinModelPortal	A2QTN4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00007807; CADANGAP00007665; CADANGAG00007807.
GeneID	4983805.
KEGG	ang:ANI_1_296084.
Phylogenomic databases
HOGENOM	HOG000176257.
KO	K11427.
OrthoDB	EOG412QDV.
Family and domain databases
InterPro	IPR013110. DOT1. IPR025789. Histone_H3-K79_MeTrfase. IPR021162. Histone_H3-K79_MeTrfase_fungi. [Graphical view]
Pfam	PF08123. DOT1. 1 hit. [Graphical view]
PIRSF	PIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
PROSITE	PS51569. DOT1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A2QTN4_ASPNC

Accession

Primary (citable) accession number: A2QTN4

Entry history

Integrated into UniProtKB/TrEMBL:	March 6, 2007
Last sequence update:	March 6, 2007
Last modified:	January 9, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)