G2RBD0 (G2RBD0_THITE) 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:

THITE_2119121 EMBL AEO69101.1

Organism

Thielavia terrestris (strain ATCC 38088 / NRRL 8126) (Acremonium alabamense) [Complete proteome]

Taxonomic identifier

578455 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › Thielavia › Thielavia terrestris

Protein attributes

Sequence length	495 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 EMBL AEO69101.1 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)
	G2RBD0 [UniParc]. Last modified November 16, 2011. Version 1. Checksum: 38AAE565CFBDD62D	FASTA	495	54,951
	10 20 30 40 50 60 MSIFSKRSKF RVPTEVRRIK QVVEPVAQPK TARAAILGST AAPAAASHSV SRSSHGTPRA 70 80 90 100 110 120 SPKPASSSRT QALQSAMSSP ELRRSSTTTS RKRRAAYTNS PLNDSDPESD DEDWRETLDP 130 140 150 160 170 180 SKRRKRAHTE DPARQLRHPR LWAGQNEEED ELGIVHAVEV ASLADKCRPV MGLEEDEVGV 190 200 210 220 230 240 RLRYPGANYL ERYELVWGRD KIDGARDIME VVNLVGSIYL TDAQAKPFLD QDHGIYRRLE 250 260 270 280 290 300 KSKNTKDGKG FKAALQEYNE QLLALQKKGA IAQNIDAMRG VPRELVETIL RQVYDRTVAP 310 320 330 340 350 360 KVELLAKYQN GTDNVYGELL HPFVSDIFDR TKLTSEMVFV DLGSGVGNVT LQAALERGCE 370 380 390 400 410 420 SWGCEMMENA CNLAEAQQKE FAARCQLWGI APGKVHLERG DFCKNERTLA ALKRADVVLV 430 440 450 460 470 480 NNQAFTSELN GTLVNMFLDL KVGCKIVSLK TFVHDNKTAA NDVAASILDV EHFSYPGGYV 490 SWTAAPGTFC ISTRK

References

[1]

"Comparative genomic analysis of the thermophilic biomass-degrading fungi Myceliophthora thermophila and Thielavia terrestris." Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I., Ishmael N., John T., Darmond C., Moisan M.C., Henrissat B., Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P. , Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J., Paulsen I.T., Elbourne L.D., Baker S.E., Magnuson J., Laboissiere S., Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W., Tsang A. Nat. Biotechnol. 29:922-927(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38088 / NRRL 8126.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003012 Genomic DNA. Translation: AEO69101.1.
RefSeq	XP_003655437.1. XM_003655389.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	11520350.
KEGG	ttt:THITE_2119121.
Phylogenomic databases
KO	K11427.
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

G2RBD0_THITE

Accession

Primary (citable) accession number: G2RBD0

Entry history

Integrated into UniProtKB/TrEMBL:	November 16, 2011
Last sequence update:	November 16, 2011
Last modified:	January 9, 2013
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)