位置:首页 > 蛋白库 > DOT1_CANAL
DOT1_CANAL
ID   DOT1_CANAL              Reviewed;        1343 AA.
AC   Q5A309; A0A1D8PKG3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=CAALFM_C306300WA; ORFNames=CaO19.7402;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017625; AOW28637.1; -; Genomic_DNA.
DR   RefSeq; XP_716067.1; XM_710974.1.
DR   AlphaFoldDB; Q5A309; -.
DR   SMR; Q5A309; -.
DR   STRING; 237561.Q5A309; -.
DR   PRIDE; Q5A309; -.
DR   GeneID; 3642236; -.
DR   KEGG; cal:CAALFM_C306300WA; -.
DR   CGD; CAL0000184097; DOT1.
DR   VEuPathDB; FungiDB:C3_06300W_A; -.
DR   eggNOG; KOG3924; Eukaryota.
DR   HOGENOM; CLU_004528_0_0_1; -.
DR   InParanoid; Q5A309; -.
DR   OMA; HCESFIL; -.
DR   OrthoDB; 333411at2759; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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   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..1343
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-79
FT                   specific"
FT                   /id="PRO_0000270606"
FT   DOMAIN          987..1304
FT                   /note="DOT1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1110..1113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   BINDING         1133..1142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   BINDING         1160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   BINDING         1197..1198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
SQ   SEQUENCE   1343 AA;  155678 MW;  D4DE4546A3DD562C CRC64;
     MISGHLQTPD SSDHSGDEAK LTKPSGLESK TNELWSSDLE EELESRIMQP ATFSSILKQF
     PSISEETIIS KIMSNKNCDK NNWKKKIYCY RYFLQPSKEE PDVGNMKSLV EKLEKLKLKK
     WSASEIEQLF CNYLEDLTTS AVKVSIPGKT LDEVAAAVNN IHPRPRWTRK EIECLIKNEN
     DFKKLEKDLF VRDLDSIKKK IRRDNLSIQN EIQDSEKKSP QSTDSNNKDS SRDLSRKERD
     QLKKLLSKPI CFSELLAKFP GHSWEYIARE IIQLDSSEDN TIWLKKIYYY CVVYSISVDK
     EITKYIGGGN RIYEKVRSDW SKIKTLDFFK DWSLQEFERL YCFAFHDLTK SALTKNFPSK
     NLNDICKVVN ISFPKVPYTD REMKYLERHL DTPMQTLENN LPFRSRGSIH KKLEALKALT
     ETTEQKQPPT KTRPKNEEEK NVENAAYMKE LIMFDLTLEA IENTFPSEPI EEIIKEIKNS
     EIFDPLSFTR GEKELMAKLV KKGNLIDDCF DYFPLREEEF IRSKYAEAEY VSGRKMKFNT
     PEERLAYEAK WTLFNMGKQE YGRGNRRSTK RYCEIDELSK LEQEASVKRS KKKIELTEEE
     LEQRRKRSEH FRLCRLKKLE EKREKYRIEK AKRLEKIAAG LIKPSTSGYE LKDIVTSAEY
     FQSIVGDKQK VQEGQKRKRI QTEYFAPEFI EKPKAVKLKT TKRQAEKNKI KKQLKREAQL
     KIKKKKTIAP KKGKRRVKTN NGIIEEIKDV YKLSSEPYVE SEVEEEDEEE DYISPYDPPD
     IISDSQVKLN GRHLYISSFY KELPEIPELK FVSLPHMEMS GNDITVAKQI MTTANDDILY
     DDCLAYEIVA QHIKSYRDLP ISFPPVLDPI THELNSANIV RIRFFLYPEH YESFMLASPK
     SNELDPVHEI AKLFMIQYSL YFSHSDTLKK IITEDYCHKL EHSVEENDFG EFMFVVDKWN
     QLVMKLSPNL ASVQNILGLK EDINEAPRAY LNQQEVSIPT NSDLKIETFY DEIMYESASP
     LFNPINSNLE IDSESAPIPL GEVEIPNNVI EEINEKMPDN YIPDFFRRLK EKTEVSRYAM
     QQILLRVYSR VVSTDSRKLR SYKAFTAETY GELLPSFTSE VLEKLNLLPT QKFYDLGSGV
     GNTTFQAALE FGACSSGGCE IMEHASKLTE LQAGLIQKHL AVLGLQKLNL DFALHESFVG
     NEKVRASCLD CDVLIINNYL FDGQLNDEVG KLLYGLRPGT KIVSLRNFIS PRYRATFDTV
     FDFLSVEKHE MSDIMSVSWT ANKVPYYIST VEETIPREYL SREETKETSG KSKSVSPVGE
     IENVAAAMMT PPTDSSESEI IKN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024