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Database: UniProt
Entry: C9ZHT8_TRYB9
LinkDB: C9ZHT8_TRYB9
Original site: C9ZHT8_TRYB9 
ID   C9ZHT8_TRYB9            Unreviewed;       275 AA.
AC   C9ZHT8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   08-NOV-2023, entry version 47.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|RuleBase:RU271113};
DE            EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190, ECO:0000256|RuleBase:RU271113};
DE   AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821, ECO:0000256|RuleBase:RU271113};
GN   ORFNames=TbgDal_I40 {ECO:0000313|EMBL:CBH08809.1};
OS   Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH08809.1, ECO:0000313|Proteomes:UP000002316};
RN   [1] {ECO:0000313|Proteomes:UP000002316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX   PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA   Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA   Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA   Barry J.D., Berriman M., Hertz-Fowler C.;
RT   "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT   chronic human african trypanosomiasis.";
RL   PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC   -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC       histone H3 to form H3K79me3. This methylation is required for telomere
CC       silencing and for the pachytene checkpoint during the meiotic cell
CC       cycle by allowing the recruitment of RAD9 to double strand breaks.
CC       Nucleosomes are preferred as substrate compared to free histone.
CC       {ECO:0000256|RuleBase:RU271113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA-
CC         COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360;
CC         Evidence={ECO:0000256|ARBA:ARBA00001569,
CC         ECO:0000256|RuleBase:RU271113};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU271113}.
CC   -!- MISCELLANEOUS: In contrast to other lysine histone methyltransferases,
CC       it does not contain a SET domain, suggesting the existence of another
CC       mechanism for methylation of lysine residues of histones.
CC       {ECO:0000256|RuleBase:RU271113}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. DOT1 family. {ECO:0000256|RuleBase:RU271113}.
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DR   EMBL; FN554964; CBH08809.1; -; Genomic_DNA.
DR   RefSeq; XP_011771250.1; XM_011772948.1.
DR   AlphaFoldDB; C9ZHT8; -.
DR   SMR; C9ZHT8; -.
DR   GeneID; 23858437; -.
DR   KEGG; tbg:TbgDal_I40; -.
DR   VEuPathDB; TriTrypDB:Tbg972.1.40; -.
DR   OrthoDB; 117288at2759; -.
DR   Proteomes; UP000002316; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025789; DOT1_dom.
DR   InterPro; IPR030445; H3-K79_meTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21451; HISTONE H3 METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR21451:SF0; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 1.
DR   Pfam; PF08123; DOT1; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51569; DOT1; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU271113};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU271113};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU271113};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU271113};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU271113}.
FT   DOMAIN          1..275
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
SQ   SEQUENCE   275 AA;  30887 MW;  7DAB217F01B2979F CRC64;
     MDARVHRSKR GCGRVLKRSR ASSPEVVAEV GTGRPGDPFV LPLRSSPNGS GCHHCPEHSC
     DCLYVSKELE RCYLSLQVSR QVTCKGRREL CAKSVLPPFV ARLLRVANVT ADDTFYDLGC
     GNGSVLFHVA LATGASCVGV EINEHNAKVA KEAWTHLRPV FEKRRGRKLD VSIVCGDFCK
     VLKQDNYFSS SCVVWIANLL MPRFVNHYLS ERLRSLPIGS RVLCMEDLYP HSRSVAAARD
     PDAFEKFEMV DYRWQEDSVE WSPASGPFYL YIKRS
//
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