DOT1_CANGA
ID DOT1_CANGA Reviewed; 652 AA.
AC Q6FNM5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific;
DE EC=2.1.1.360;
DE AltName: Full=Histone H3-K79 methyltransferase;
DE Short=H3-K79-HMTase;
GN Name=DOT1; OrderedLocusNames=CAGL0J10516g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000250|UniProtKB:Q04089}.
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:0000250|UniProtKB:Q04089, ECO:0000255|PROSITE-
CC ProRule:PRU00902};
CC -!- ACTIVITY REGULATION: Ubiquitination of histone H2B to form H2BK123ub1
CC is required for efficient DOT1 methyltransferase activity on histone
CC H3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. DOT1 family. {ECO:0000255|PROSITE-ProRule:PRU00902}.
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DR EMBL; CR380956; CAG61120.1; -; Genomic_DNA.
DR RefSeq; XP_448169.1; XM_448169.1.
DR AlphaFoldDB; Q6FNM5; -.
DR SMR; Q6FNM5; -.
DR STRING; 5478.XP_448169.1; -.
DR EnsemblFungi; CAG61120; CAG61120; CAGL0J10516g.
DR GeneID; 2889607; -.
DR KEGG; cgr:CAGL0J10516g; -.
DR CGD; CAL0133274; CAGL0J10516g.
DR VEuPathDB; FungiDB:CAGL0J10516g; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_027287_0_1_1; -.
DR InParanoid; Q6FNM5; -.
DR OMA; NSVSWTH; -.
DR Proteomes; UP000002428; Chromosome J.
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:0031151; F:histone methyltransferase activity (H3-K79 specific); IEA:EnsemblFungi.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR GO; GO:0034729; P:histone H3-K79 methylation; IEA:EnsemblFungi.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0031452; P:negative regulation of heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR GO; GO:0006301; P:postreplication repair; IEA:EnsemblFungi.
DR GO; GO:0000725; P:recombinational repair; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.150; -; 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; PTHR21451; 1.
DR Pfam; PF08123; DOT1; 1.
DR PIRSF; PIRSF017570; Histone_H3-K79_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51569; DOT1; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Methyltransferase; Nucleus; Reference proteome;
KW Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..652
FT /note="Histone-lysine N-methyltransferase, H3 lysine-79
FT specific"
FT /id="PRO_0000270607"
FT DOMAIN 321..638
FT /note="DOT1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT REGION 15..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 442..445
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT BINDING 465..474
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT BINDING 492
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT BINDING 529..530
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
SQ SEQUENCE 652 AA; 74615 MW; 2A94C532FB090699 CRC64;
MQEGLKLAER YNASLGSSQT YPIDNHHDKE SSTDVATDDI MEKDLHSGKT ISSQNSLDGS
EASTPVHQLE RPTIDVSERN DSRRKFRKKT SLDDLLDQAS KFQPQYEYSF PTSFLRKRKA
PQSNESDGEE EAKQNRTNKI VKQKKTKKNV KVTSKSKASV PIEEKHTINK QPKKTGTGGM
KRGPKPGRKK KSQKNTKNSI KKESTNAINN HKMYEMDSAS SRFAEHKNST NSESANNSFI
DWSLPKFSPP YQIFDIDNIN SYSNFQGQIY SSASLTKHHN EIGSKTPFSR NRDGSKSPID
DGQGKLIGLR SILYPDYYEE YLMDYKKVNF RYDGMAEIGK IMEYVGRIYL PEKYQKEYKE
TVVDIYNTAY DNKDLALSIS TVEKYNQFVG SIPKAEIVNH LAATKELPRS FLHDFLQIVY
TRSIHPYASK LKQYKAFSNY VYGELLPGFL TDVYSKCGLS KNHLFMDLGS GVGNCVIQAS
LEFGCRESFG CEIMEAASEL TEIQMREYSN RCKLFGFKQS KIDYSLRKSF INNEKVESLI
PECDVLLVNN FLFDGKLNYE VTKLLQKTKV GCKIISLKNI RASGYTLDTV NIESVLNRLE
VKKYRLDNNS VSWTHNGGEY FISTVLDRID ESLLDPQKRD RRNTHRPAKY TR
