ID C5M9R9_CANTT Unreviewed; 1369 AA.
AC C5M9R9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 72.
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=CTRG_02231 {ECO:0000313|EMBL:EER33413.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER33413.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER33413.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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; GG692397; EER33413.1; -; Genomic_DNA.
DR RefSeq; XP_002547934.1; XM_002547888.1.
DR STRING; 294747.C5M9R9; -.
DR EnsemblFungi; CTRG_02231-t43_1; CTRG_02231-t43_1-p1; CTRG_02231.
DR GeneID; 8296934; -.
DR KEGG; ctp:CTRG_02231; -.
DR VEuPathDB; FungiDB:CTRG_02231; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_004528_0_0_1; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000002037; 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; 1.10.260.170; -; 2.
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:UP000002037};
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 1009..1330
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 13..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1369 AA; 157940 MW; 4E1D1C98A6B1AE60 CRC64;
MVSLGSIFSS VRSLTSEPMV SPPADKVMEE KQLNIQDEKE SDIPTVDSNV HLQTPDMSDQ
SCDEAKLNSE PDEASTTWTK DLENELKQLA GQSITFSKVL THFPGFDWKD IGEKILKTKI
NNSLWKRKLV CYDQLFKHEK AFVIRAHSGI LSRIDDKKLK SWKNHEIEQL LCNLYEDLTT
DGVKASLTNK SLKQVAEAIH VVAHVVSWTP KELQFLMDNF EDQENLKKGL FFRSSDSIYN
KLRLTNQLST TAKSSGKSKH EDALNKISTL PISFSKVMEQ FPAGDWKDIA TTLYKLTADN
ESSNWSQKIG CYCLVNHFDQ FAREEIDDEF LTSIGYTKNE FKKFRNNLCK ALALPEFKKW
STKEFEDFYS LSFHDLTRDT LRQKFPKKNL TDMKKFVSVF DSQRNNFNSG EITYLEQNSD
AKISELMLHL PCRSKKSIYK ALDDLNNPES EENPVLLQLL QHDLTIDTIK ENFPDEDIES
IINDIKNHPE FDKDMFTKGE KELMNSFVHA NKNVEECLKH FPVRDEKSIR RLHNESQYLS
GRKVKFESPE ERLAYEAKWT LIATGSSNSS RSKRALKRSA DFEEFTKLEQ EVAVKHIKKP
KPELTEEELA LRREKQEKAR LARERKKEER RKLIELRKSE KKPKPKKQTT SNELKDLLTG
AEYFQSTVGD RKQVQEGEKR KRVQPEHYEP EIRHSNNPVK LKTTNRQAEK IRIKKELQRK
ARAEKEKELA IKSKNQIKQL NSKRKKQQSQ KRSKSKIPDD DEIIAEIKRI YNMEAEQQQL
DDSEEEEEFI SPYDPPDITS DSFVKLNGRQ LYVSDFYSEE PSIPQLEFVH MEQNDENNED
SKVKTMSPGK SIMTAADDKI LYEDNLALEI VTTHMRSYRD MPISFPPILD PVTKEINPLN
IIKIRFLLYP EHTESFILAS PKSNELDPVQ EIAKLFMIQC SLYFSHSEVL KNIIMEDYCK
KLENSIEEND FGEFMAVIDK WNQLVLNLSP NTSSSQKILE SGEDINSAPR YYLNEEEVKT
PTVADLKLDT FYEEIMYESA SPSFQPIEIK FGDDITVPDT NNEVSYDNVD IPTNISQVSR
IIKPEGYNTD FFKRLQEKTD VSRYTIQQIL LRIYSRVVST DSRKLRSYKA FTAEVYGELL
PSFTSEVLEK VNLLPGQKFY DLGSGVGNTT FQAALEFGAS PSGGCEIMDH ASYLTTLQTG
LIQKHLSVLG LRKLDLDFEL HSSFVNNEKV RQSCLECNVL IINNYLFDGP LNAEVGRLLV
GLKPGTKIIS LRSFISPRYR ATFDTVFDFL RVEKHEMSDV LSVSWTANKV PYYISTVEES
ILKEYLSKEE TADISERSKS SSPVHDFGGN RNSMLTPPTD SSELENYKE
//