ID   G0VGI5_NAUCC            Unreviewed;       630 AA.
AC   G0VGI5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|PIRNR:PIRNR017570};
DE            EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190, ECO:0000256|PIRNR:PIRNR017570};
DE   AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821, ECO:0000256|PIRNR:PIRNR017570};
GN   Name=NCAS0F01220 {ECO:0000313|EMBL:CCC70606.1};
GN   OrderedLocusNames=NCAS_0F01220 {ECO:0000313|EMBL:CCC70606.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC70606.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC70606.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR017570}.
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|PIRNR:PIRNR017570};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR017570}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. DOT1 family. {ECO:0000256|PIRNR:PIRNR017570}.
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DR   EMBL; HE576757; CCC70606.1; -; Genomic_DNA.
DR   RefSeq; XP_003676961.1; XM_003676913.1.
DR   AlphaFoldDB; G0VGI5; -.
DR   STRING; 1064592.G0VGI5; -.
DR   GeneID; 11527634; -.
DR   KEGG; ncs:NCAS_0F01220; -.
DR   eggNOG; KOG3924; Eukaryota.
DR   HOGENOM; CLU_027287_0_1_1; -.
DR   InParanoid; G0VGI5; -.
DR   OMA; NAKVGCK; -.
DR   OrthoDB; 146338at2759; -.
DR   Proteomes; UP000001640; Chromosome 6.
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; 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|PIRNR:PIRNR017570};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR017570};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR017570};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR017570};
KW   Transcription {ECO:0000256|PIRNR:PIRNR017570};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR017570};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR017570}.
FT   DOMAIN          284..617
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..150
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         421..424
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT   BINDING         444..453
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT   BINDING         471
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT   BINDING         508..509
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
SQ   SEQUENCE   630 AA;  71757 MW;  8B0BC9ACFD232324 CRC64;
     MTTNTVPFTP SPSSSSIFST STTNFNNNNS RDSSMAPADS TEASLTEQTK KGKTRAKGSS
     AVEKLLEEAN RYHPQYEYSL PQGFLRTRKS KAASPSEEQA SDLAKDDNLV KRKMEEEEDY
     DTSTTAAKKV RKNKVTSTSS TKKRKRKIKK AETNGTTGSK PTKKRKDTIK RPLSPSAALA
     DSVRRMSISA MLDDSDTKDG TGIYNEQGVK LDPVANKDDR AMTSTFLDWD QPYLELQYPL
     FNVDSLKLTN VYKGNPIKST ILTSLTHHQS RHKPPSLSND SSIKFVHLQS PLFVNYQEEY
     MINFEKDLQR YNPMSEIGKL IEYTALVYLP STYSEKLKRE VIPSLNQAFD NSDTDRFISS
     VERYNSIIRM VPRHEILEHL KTITQIPKSF IHDFLHIIYT RSIHPHASKL KHYKAFSNFV
     YGELLPNFLS EVFSQCNLKP NCTFMDLGSG VGNCVIQASL EYGLKKSFGC EIMPDASELT
     ELQMVELKER GKLFGFNLSD IEFSLRESFV DNPKVDELIK DCDLLLVNNF LFDSKLNEKV
     EKITQNLKTG CKIVSLKNLR SFSYKIDFFN MENILSRLKV EKVLLKEDSV SWTHSGGEYY
     IATVMENIDE SLFDPVVRGR NTRRPTKYSR
//