ID A0A024GSJ8_9STRA Unreviewed; 329 AA.
AC A0A024GSJ8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987};
DE EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190};
DE AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821};
GN ORFNames=BN9_108610 {ECO:0000313|EMBL:CCI49523.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI49523.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI49523.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI49523.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI49523.1}.
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DR EMBL; CAIX01000307; CCI49523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GSJ8; -.
DR InParanoid; A0A024GSJ8; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
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.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 130..274
FT /note="DOT1"
FT /evidence="ECO:0000259|Pfam:PF08123"
SQ SEQUENCE 329 AA; 37544 MW; D464F2FCC2036D30 CRC64;
MSFSGFDNFD KILLAFSQQA TKCQKYDPND EDWQQLLQLS TYVRKEVAQL LQEPKGQQIL
KDSNALEKIK SLIPDSAKAE LENMKVQDFA LTILYEQPFQ FFSKVYHGFG SEYGKELSMQ
AREDANINES SYIYGEIDFF AFVDVLQWVI RQGSIMKNEA VFYDLGSGTG KAVIAASLLY
NFDKVIGIEA LEPLNTFAKK RAVKLRNLTK NNCLASSIEF WYGSFLEKDW TDGTIVFCHA
TCFSDSDWRS ISLVAEKLKQ GSYVITASQI LQSALFEVVK SEQVKTSWGT AKIYIHRRRN
IGRWASKILR GGRASRLDWK PEVKDSILD
//
