ID W6KFC1_9TRYP Unreviewed; 296 AA.
AC W6KFC1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=GSEM1_T00000317001 {ECO:0000313|EMBL:CCW59778.1};
OS Phytomonas sp. EM1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW59778.1, ECO:0000313|Proteomes:UP000027080};
RN [1] {ECO:0000313|EMBL:CCW59778.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW59778.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW59778.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW59778.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
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|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; HF955061; CCW59778.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KFC1; -.
DR EnsemblProtists; CCW59778; CCW59778; GSEM1_T00000317001.
DR OrthoDB; 117288at2759; -.
DR Proteomes; UP000027080; Unassembled WGS sequence.
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:SF24; 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|RuleBase:RU271113};
KW Nucleus {ECO:0000256|RuleBase:RU271113};
KW Reference proteome {ECO:0000313|Proteomes:UP000027080};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU271113};
KW Transferase {ECO:0000256|RuleBase:RU271113}.
FT DOMAIN 1..296
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 11..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 33635 MW; DC25891C70B8242F CRC64;
MLKHLCHGEA AAQQGVKGKR ARPAVLSPTP HRLRKGAQAH EGRTGPLEKK EEEGRWEEDP
THLPLRTTPN RSGCRHCPTP RCVCVWLADA LAGCYAALPA KRQLQQRGRR ELCAKSVLTP
FVSRLVRLAR LRPGETFYDL GCGNGSVLFQ VALMTGVRCV GVEINPTNAE VARAAWEELR
PTLERRCRRR LDIEIRCADL CEVLKGEEVV SAPCVIWAAN LLLPKATNHY LSERLRACAV
GTRIFCFEDL YPHNRSITRV RDPDAFERFE MKDFVWQPMS VEWCDLEGDF YLYTRK
//
