ID   C4XZ66_CLAL4            Unreviewed;      1117 AA.
AC   C4XZ66;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|RuleBase:RU271113};
DE            EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190, ECO:0000256|RuleBase:RU271113};
DE   AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821, ECO:0000256|RuleBase:RU271113};
GN   ORFNames=CLUG_01248 {ECO:0000313|EMBL:EEQ37125.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ37125.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ37125.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ37125.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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|RuleBase:RU271113}.
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|RuleBase:RU271113};
CC   -!- ACTIVITY REGULATION: Ubiquitination of histone H2B to form H2BK123ub1
CC       is required for efficient DOT1 methyltransferase activity on histone
CC       H3. {ECO:0000256|RuleBase:RU271113}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU271113}.
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       {ECO:0000256|RuleBase:RU271113}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. DOT1 family. {ECO:0000256|RuleBase:RU271113}.
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DR   EMBL; CH408077; EEQ37125.1; -; Genomic_DNA.
DR   RefSeq; XP_002617789.1; XM_002617743.1.
DR   AlphaFoldDB; C4XZ66; -.
DR   STRING; 306902.C4XZ66; -.
DR   GeneID; 8498996; -.
DR   KEGG; clu:CLUG_01248; -.
DR   VEuPathDB; FungiDB:CLUG_01248; -.
DR   HOGENOM; CLU_004528_0_0_1; -.
DR   InParanoid; C4XZ66; -.
DR   OMA; NFIPPRY; -.
DR   OrthoDB; 146338at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
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.
DR   PROSITE; PS51569; DOT1; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU271113};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU271113};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU271113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU271113};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU271113}.
FT   DOMAIN          800..1117
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  128265 MW;  8E851EADEBAAB35D CRC64;
     MQCSSSVSTI MGSPKPESKD SLPLYRTVPM KVSSLLNSES GETVETMPIS PDSLKVENEH
     SISPSIAKES TPASVKSDDY ESVSDELKKL TYTNLLRSHV QKRLPDVDWD EIVRYVETLT
     LPTDFTKPEI ELIVSEWYKE GPVNHRMLEY ECFARTRREI HSKICALEDL YGLKREELEC
     SQIIAMEVCN ELQLFLLSDI KPMLPHMSTS NIAGMISKHY KYKNRWSDRE VEFISDCIER
     EESRESILEA LVFRKPYEIR NKIDSVKRRL RRQSTPPIKK EPSPVVIAYE SKLSELMNSD
     LTLTGIRSVM GSRNLNRVVQ DIQSRKKRDI ALPFTYPETE FLRHSLTNNM PMADIMKELV
     IRSEEEVVAK LKTLQMACVR QKKFTNTVER LIYEAQWYMA IADGESGGRP KRRTRNNVEL
     DDLRKEALTK KKKVERTLTP EEISEKQKRS EIRTQRRIES LRRKAEENEL RKKKASMRGR
     KLRSTRKQEA ESRVAALIEE ARWFQSVTGD GTCVKEGEKR KRRPVFHLVP EFKNRQQLKN
     AQKRLVEKKK EVKKKRGRGR PRRTPSSDVD DSTSDSDSED DLEKLQHAID SDESDEFACV
     SSFDPTDIIH DSLVPLSGRQ LFNNAITSGS VNPQPVSFSD DVSVMIQSNQ YLPVNDTVAA
     KVIKDHIKSY KPLGASFPPL FTSDVNGSDV INSRNIIHIR YLLYPQHTEQ FVLAAPKSNE
     LDPVFELQKI FQIHYALFFS HSSLIKDIIY ENYCKSLERA VEEDNFSDFM TIIDQWNTLM
     LALSPYPVKF DPSIDINEAI RLYLPSNYKF QPTVSDLKLD IFYYDVLSAG EIKDSDKETS
     IDRATSPLMR PTGPIKDADS AIANIITRFR NLRPLSYPNA FIRSLQRVSE ISRFAIQQIL
     LRAYTRIVSP NSRKLRSYKA FTAEVYGELL PSFVSEVLTK VDLKPEHSFY DLGSGVGNTT
     FQAALEFGVK ESGGCELMNH ASELTSLQEI FMQKQLIVFG LKPLPLHFAL NQSFVNNPEV
     RSKCVGCDVL IVNNYLFDFP LNVEVGKLLY GMRPGSKIIS LKNFIPPRYK AGTEKTIFDY
     LKVEKHEMSD YLSVSWTANK VPYYISTVQE SVQQEYV
//