DOT1_CRYNJ
ID DOT1_CRYNJ Reviewed; 644 AA.
AC P0CN14; Q55K55; Q5K9E4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=CNK02230;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017351; AAW46180.1; -; Genomic_DNA.
DR RefSeq; XP_567697.1; XM_567697.1.
DR AlphaFoldDB; P0CN14; -.
DR SMR; P0CN14; -.
DR STRING; 5207.AAW46180; -.
DR PaxDb; P0CN14; -.
DR PRIDE; P0CN14; -.
DR EnsemblFungi; AAW46180; AAW46180; CNK02230.
DR GeneID; 3254655; -.
DR KEGG; cne:CNK02230; -.
DR VEuPathDB; FungiDB:CNK02230; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_027287_1_0_1; -.
DR InParanoid; P0CN14; -.
DR OMA; MWGVSMG; -.
DR OrthoDB; 649516at2759; -.
DR Proteomes; UP000002149; Chromosome 11.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0034729; P:histone H3-K79 methylation; IEA:InterPro.
DR GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:InterPro.
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..644
FT /note="Histone-lysine N-methyltransferase, H3 lysine-79
FT specific"
FT /id="PRO_0000270610"
FT DOMAIN 297..637
FT /note="DOT1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT REGION 25..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
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 491
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT BINDING 528..529
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
SQ SEQUENCE 644 AA; 71286 MW; FC3F9595D4D52BB6 CRC64;
MFSFFGDESK LPASTVMVSR MTVKKQAVAR QQSSGPMAGP SKPSNVTPKH SHGSLKGTPR
SASEKGTPKQ GPSSSSKSTS KVKQEERIRL STIPRTPASS SSPGRLKRKT PKVQVVESES
SSGSESSDGA LDSKPKRPKV TRKETGIDMT PLPGEEVVGR RVFCWDKVDM RGEWGRGWAG
FVGCDEVVRG NVQGWANGGG GDGSKNLGKY RAFFPQEGFD RDGDFLPSVE VLYPAKGCRE
KFVLMVPSSD REFNPIGELR NTLRLILEHY IPPSHRHIFG TLAESLDISN PLSSLPSRMT
TPLPNSLVTP PPDPASPSPA FAFEISATST PAPSTERQET IADLIRKSLA PNRRDGPLFV
TAIERYNSAM QAIQEDGTLQ QWLDEGMNGG KGIKVREWAA LVDFVHDQAY SRVVGGYSHE
LEHHPKHPEE VSKAISGKED AYGELRHAFM SKIIEQTKLG PDSVFVDLGS GVGNCVLQAS
LQAGSRSYGF ELLPVPAHCA RLQVREVQRR WAMWALKGNL DVEVHEGDFR VHKEVGRRLR
EADVVLVNNE VFPSSLNMDL ADMFLDLKEG AKIVSLKPFV PEGFRMNESN CDSFAAILRS
TQHDYYRDWV SWKGEWGNYY VAVIDRSRRI KFEESMKGRA SRRR
