DOT1_DEBHA
ID DOT1_DEBHA Reviewed; 1172 AA.
AC Q6BTC8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=DEHA2D01694g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382136; CAG86674.2; -; Genomic_DNA.
DR RefSeq; XP_458542.2; XM_458542.1.
DR AlphaFoldDB; Q6BTC8; -.
DR SMR; Q6BTC8; -.
DR STRING; 4959.XP_458542.2; -.
DR EnsemblFungi; CAG86674; CAG86674; DEHA2D01694g.
DR GeneID; 2901204; -.
DR KEGG; dha:DEHA2D01694g; -.
DR VEuPathDB; FungiDB:DEHA2D01694g; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_004528_0_0_1; -.
DR InParanoid; Q6BTC8; -.
DR OMA; NICEEYV; -.
DR OrthoDB; 333411at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034729; P:histone H3-K79 methylation; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
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 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..1172
FT /note="Histone-lysine N-methyltransferase, H3 lysine-79
FT specific"
FT /id="PRO_0000270611"
FT DOMAIN 846..1172
FT /note="DOT1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 981..984
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT BINDING 1004..1013
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT BINDING 1031
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT BINDING 1068..1069
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
SQ SEQUENCE 1172 AA; 135295 MW; 29163B7AA796D97B CRC64;
MENIAHHNTT YNITPICSDS SECSSMEMLP LGCKTHSDKS DARRNLMDTG IYTPDSNSDS
SDPRSDSSCV DVSNSLAVSH PISFCNWTDE ESSLLTEHIK TDLTSEALTS AFPNKSLALI
IRKIHDLQPV LDWTKNEIYL LAGIILNDSN SAIRRHKHKF PCRNVSNLNK KFQHYKNMVR
RLNGVDHSKW TKPEIASLIS LIDYDLTKTK LQKELPNKNI EEIKDLTNEM RIHSNFSHVE
SVLFEQTMTE NDPIEIVLDQ FPLKNKETCK KRLLKLNELS QHRDMAKRRL DEFESLIQNE
LKQIKDSIDL TRLKYLLVND LTGKQLRSSF PGISMKYLKL IAKEMGFDEA GEYTLAEMNF
LKKALQENAK LKSIIDELPF RSQLSIETKI NSVEPNRRRS VFTSQVDELL YMAKWYSSDN
FGNLSRRRNS RYASKLDKPK DKASDIMQPS KLHLENEEVT EAKVIPHDKG VENMISDHKL
KGKNNEQKKR KSKKPTSMVE VLKEESAYFQ SVTGNRCVLK EGQKRKRERL MQIKLETKLK
KPKSQNLNET NRIQETKKLM KCDVEPDKVK EQKSFKSENL KEAKLDASDS SIVSDVEISL
KKKLNKIENE EKRSPYDPED ISTDTLVPLY GRQLYVNEVY ETQPRPPKLS FREDTNIMVQ
NCSEISLTDT IAADIISQHC KNYRDMPISF PSLTIVDRNT NRMILNPMNK IRIRFLLYPQ
HSELFILAEP KSNELDPINE IKKLFQLHYS LFFSHSSKLK KIILSEYNKE IDISIEENDF
VRFMFVIDKW NRLMVELTPN DVDIGSHDIN EEIRAYLSPN EIKIPSDEDI RLDIFYSEIQ
LSTEENPISD NDPIEPSSPS FDLIKSMKRC FTHDSSNRLT PPISSEEDNK ENEPPIESDF
RNNNNKGSIP CTPVRLNTRN KMVVNAVKPE NYESNFFRHL KEKTSVSRFC VQQILLRIYS
RIVSTESRKL RSYKAFTAEV YGELLPSFTS EVLTKVNLQP QHKFYDLGSG VGNTTFQAAL
EFGVHLSGGC EIMEHASKLT ELQTMLLNKH LALLGLKKLP LNFALSQSFV ENDIVRQAVI
ECDVLLVNNY LFDVNLNTAV GKMLYGLKPG TKIISLRNFI RPRYKASSDK TIFDYLKVER
HEMSNYLSVS WTANKVPYYI STVQENICEE YV
