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Protein

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

Gene

SS1G_03126

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Status
Unreviewed-Annotation score: Annotation score: 2 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

Enzyme regulationi

Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3.UniRule annotation

GO - Molecular functioni

  1. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulatorUniRule annotation, MethyltransferaseUniRule annotation, Transferase

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:SS1G_03126Imported
OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)Imported
Taxonomic identifieri665079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
ProteomesiUP000001312: Unassembled WGS sequence

Subcellular locationi

Nucleus UniRule annotation

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

NucleusUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi665079.A7ECT7.

Structurei

3D structure databases

ProteinModelPortaliA7ECT7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.UniRule annotation
Contains 1 DOT1 domain.UniRule annotation

Phylogenomic databases

eggNOGiNOG294902.
InParanoidiA7ECT7.
KOiK11427.
OMAiFPFISRI.
OrthoDBiEOG7KH9VN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025789. DOT1_dom.
IPR013110. DOT1_dom_Pfam.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF08123. DOT1. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51569. DOT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A7ECT7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLNFGQKNL TIKPVVPKYK IETIKVPKQS PRPILPTRTS SNNLRTGAPA
60 70 80 90 100
TKVADARGRL AISTSNSGAG KKRKEREISG SRGVGKNSNL KARRSPSQRP
110 120 130 140 150
LQTDSEEDEE TRIPAKRAKS ENVELDLGRS LKDQKAFSSD AADNQGSKCK
160 170 180 190 200
MIHAADVMMT KHRAKRGEKV CDRKKEEGEA VYLRYPSVRR MERYQLISEG
210 220 230 240 250
EVIDPGEEEL INPYDEIPKI AEIVKDEYLT EEQAAEFQHP ETGIIRKINK
260 270 280 290 300
ATNNITWTLA NKHKKPYDKA KLKELLVEFR NAVEVYNDAL GTLTKNGSLA
310 320 330 340 350
HNLDNKHSLS SKLLKMVLQQ VYDRAVSPQV ELTREYQNGT DYVYGELTFP
360 370 380 390 400
FISRILKEDT HMKSDQVFID LGSGVGNVVI HAALQVGCES WGCEIMENCC

LQP
Length:403
Mass (Da):45,269
Last modified:September 11, 2007 - v1
Checksum:iF2DD1270E4E296DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476624 Genomic DNA. Translation: EDO00653.1.
RefSeqiXP_001595038.1. XM_001594988.1.

Genome annotation databases

EnsemblFungiiEDO00653; EDO00653; SS1G_03126.
GeneIDi5492104.
KEGGissl:SS1G_03126.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476624 Genomic DNA. Translation: EDO00653.1.
RefSeqiXP_001595038.1. XM_001594988.1.

3D structure databases

ProteinModelPortaliA7ECT7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi665079.A7ECT7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDO00653; EDO00653; SS1G_03126.
GeneIDi5492104.
KEGGissl:SS1G_03126.

Phylogenomic databases

eggNOGiNOG294902.
InParanoidiA7ECT7.
KOiK11427.
OMAiFPFISRI.
OrthoDBiEOG7KH9VN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025789. DOT1_dom.
IPR013110. DOT1_dom_Pfam.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF08123. DOT1. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51569. DOT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
    Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
    , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
    PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 18683 / 1980 / Ss-1Imported.

Entry informationi

Entry nameiA7ECT7_SCLS1
AccessioniPrimary (citable) accession number: A7ECT7
Entry historyi
Integrated into UniProtKB/TrEMBL: September 11, 2007
Last sequence update: September 11, 2007
Last modified: January 7, 2015
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

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.UniRule annotation

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.