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Database: UniProt/TrEMBL
Entry: C5M9R9_CANTT
LinkDB: C5M9R9_CANTT
Original site: C5M9R9_CANTT 
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
//
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