ID G0WEY8_NAUDC Unreviewed; 679 AA.
AC G0WEY8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 Name=NDAI0H01750 {ECO:0000313|EMBL:CCD26349.1};
GN OrderedLocusNames=NDAI_0H01750 {ECO:0000313|EMBL:CCD26349.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26349.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26349.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR EMBL; HE580274; CCD26349.1; -; Genomic_DNA.
DR RefSeq; XP_003671592.1; XM_003671544.1.
DR AlphaFoldDB; G0WEY8; -.
DR STRING; 1071378.G0WEY8; -.
DR GeneID; 11495880; -.
DR KEGG; ndi:NDAI_0H01750; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_027287_0_1_1; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000000689; Chromosome 8.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:InterPro.
DR Gene3D; 1.10.260.170; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR021162; Dot1.
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 PIRSF; PIRSF017570; Histone_H3-K79_MeTrfase; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51569; DOT1; 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:UP000000689};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR017570-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 349..666
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 23..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 470..473
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT BINDING 493..502
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT BINDING 520
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT BINDING 557..558
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
SQ SEQUENCE 679 AA; 78114 MW; E8B95F4908155832 CRC64;
MPSAYQGSSM SATSVSLQET NVVGSPIVAT QEANDNNQEE EPSLMHNRDS KKEKNAHLNT
HDKKARNNKT RPADRELRDL LDDVTKYHPQ YDYSLPRTFL RSSTKDHKVR GKEHGVDQLG
EKETEGKSPM NQKNSSLQRL KKQRALNKAK KLDTTGQNIV KETFLAENKV NSTHNKFSSS
KRKKLVKEKD LVSVKTKKIK KRKPSPTPEA ALDSNSSTPS LSKENSIMSL TRHSESMPTP
NEGLLLPPDY NNNDDEHDKN NLFKEVATDR KEHIKEDFSS TTFVDWSKPT LKLQYPIFNI
EELSQSNFYF DELPIQSTTL TKNVYAHDPE NCKLVKLQNP LFANYQEEYH IDFNKDFEKY
NPMSEIGKII EYTTYIYLPE PFSDQIKIDI IPRLNDAFDN SEIKNFISAI EDYNSSIKRI
PRYKIIEHLA TIKEVPISFI HDFLHIVYTR AIHPNVNKLK GYKAFSNFVY GELLPSFLSE
LFGKCDLNST KTFMDLGSGV GNCVIQASLE YGCEKSFGCE IMPQVCHLTE LQQVELQRRS
KLFGFTPSDI EFSLRKSFVN NTRVDQLIPK CDVLLINNFL FDSALNKEVE KIIQNCKPGC
KIVTLKNLRS FGYTIDFFNI ENILNRLKVE RIDLKEDSVS WTHNGGEYFI ATVLENIDES
LFEPEVRSRA TRRPTKYSR
//
