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Protein

Histone-lysine N-methyltransferase, H3 lysine-79 specific

Gene

An09g02720

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei355 – 3551S-adenosyl-L-methionineUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulatorUniRule annotation, MethyltransferaseUniRule annotation, Transferase

Keywords - Biological processi

Transcription, Transcription regulationUniRule annotation

Keywords - Ligandi

S-adenosyl-L-methionineUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase, H3 lysine-79 specificUniRule annotation (EC:2.1.1.43UniRule annotation)
Alternative name(s):
Histone H3-K79 methyltransferaseUniRule annotation
Gene namesi
ORF Names:An09g02720Imported
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)Imported
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706 Componenti: Chromosome 1L

Subcellular locationi

  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

NucleusUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00007665.

Structurei

3D structure databases

ProteinModelPortaliA2QTN4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni306 – 3094S-adenosyl-L-methionine bindingUniRule annotation
Regioni329 – 33810S-adenosyl-L-methionine bindingUniRule annotation
Regioni391 – 3922S-adenosyl-L-methionine bindingUniRule annotation

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000176257.
KOiK11427.
OrthoDBiEOG7KH9VN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR021162. Dot1.
IPR025789. DOT1_dom.
IPR013110. DOT1_dom_Pfam.
IPR030445. H3-K79_meTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21451. PTHR21451. 1 hit.
PfamiPF08123. DOT1. 1 hit.
[Graphical view]
PIRSFiPIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51569. DOT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2QTN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFFDHLQKG GAFSLQPKKP QIRKVVQTRT APASRSTSQT PGPSSRTPPA
60 70 80 90 100
QLKAQQSASR SVSRDRDPPS AKRRHGTPAQ SRKRQTPELR LSSDDDASDT
110 120 130 140 150
DSSFEVRKRA RTGDSAEPDP ARRVRSLKAF SEDSVRSLPM IHAADITSRQ
160 170 180 190 200
KAGNFKPAFG AAKPLPELLL QYLSTSAPER YNLVVPRDHD DFKPIDDIVQ
210 220 230 240 250
VLDIVSQNYI PDEAADEFNN ESTGIKRRLR RALAHLSEAD FRSVVNEYNE
260 270 280 290 300
AIVRLRRDGS IAKKLDSTSR LNLPHVERIL NQIYSRTVSP RVESLRQYEN
310 320 330 340 350
GTDNVYGELL PRFISTIFKE TGLKSGQVFV DLGSGVGNVV LQAALEIGCE
360 370 380 390 400
SWGCEMMDNA CDLADLQQAE FRSRCRLWGI APGKTHLVRG DFLKEQPIID
410 420 430 440 450
VLKRADVILI NNQAFTPQLN NELINHFLDM KEGCQIVSLK SFVPAGHKIQ
460 470 480 490 500
SRNLNSPINL LKVKQRNYWS NSVSWTDVGG TYFIATKDSS RLKAFVDSMQ
Length:500
Mass (Da):55,943
Last modified:March 6, 2007 - v1
Checksum:i377590381809B001
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270196 Genomic DNA. Translation: CAK40209.1.
RefSeqiXP_001393586.1. XM_001393549.2.

Genome annotation databases

EnsemblFungiiCADANGAT00007807; CADANGAP00007665; CADANGAG00007807.
GeneIDi4983805.
KEGGiang:ANI_1_296084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270196 Genomic DNA. Translation: CAK40209.1.
RefSeqiXP_001393586.1. XM_001393549.2.

3D structure databases

ProteinModelPortaliA2QTN4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00007665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00007807; CADANGAP00007665; CADANGAG00007807.
GeneIDi4983805.
KEGGiang:ANI_1_296084.

Phylogenomic databases

HOGENOMiHOG000176257.
KOiK11427.
OrthoDBiEOG7KH9VN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR021162. Dot1.
IPR025789. DOT1_dom.
IPR013110. DOT1_dom_Pfam.
IPR030445. H3-K79_meTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21451. PTHR21451. 1 hit.
PfamiPF08123. DOT1. 1 hit.
[Graphical view]
PIRSFiPIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51569. DOT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G., Debets A.J., Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J., d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P., van den Hondel C.A., van der Heijden R.T., 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., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U., Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P., van Ooyen A.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 A1513Imported.

Entry informationi

Entry nameiA2QTN4_ASPNC
AccessioniPrimary (citable) accession number: A2QTN4
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2007
Last sequence update: March 6, 2007
Last modified: May 27, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.