SET9_YARLI
ID SET9_YARLI Reviewed; 866 AA.
AC Q6C519;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Histone-lysine N-methyltransferase SET9;
DE EC=2.1.1.372 {ECO:0000250|UniProtKB:Q9USK2};
DE AltName: Full=SET domain protein 9;
GN Name=SET9; OrderedLocusNames=YALI0E21802g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Histone methyltransferase that trimethylates 'Lys-20' of
CC histone H4 to form H4K20me3. {ECO:0000250|UniProtKB:Q9USK2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:64456, Rhea:RHEA-COMP:15554, Rhea:RHEA-
CC COMP:15998, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.372;
CC Evidence={ECO:0000250|UniProtKB:Q9USK2, ECO:0000255|PROSITE-
CC ProRule:PRU00900};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar4-20
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00900}.
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; CR382131; CAG79838.1; -; Genomic_DNA.
DR RefSeq; XP_504243.1; XM_504243.1.
DR AlphaFoldDB; Q6C519; -.
DR SMR; Q6C519; -.
DR STRING; 4952.CAG79838; -.
DR PRIDE; Q6C519; -.
DR EnsemblFungi; CAG79838; CAG79838; YALI0_E21802g.
DR GeneID; 2911957; -.
DR KEGG; yli:YALI0E21802g; -.
DR VEuPathDB; FungiDB:YALI0_E21802g; -.
DR HOGENOM; CLU_330998_0_0_1; -.
DR InParanoid; Q6C519; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IBA:GO_Central.
DR Gene3D; 1.10.10.1700; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR InterPro; IPR025783; Set9_fungi.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR039977; Suv4-20/Set9.
DR PANTHER; PTHR12977; PTHR12977; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51567; SAM_MT43_SUVAR420_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..866
FT /note="Histone-lysine N-methyltransferase SET9"
FT /id="PRO_0000281808"
FT DOMAIN 111..223
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 243..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 96798 MW; D251BA712D3BAA24 CRC64;
MITVTPGELA TIDDALTDLL LERVFYWAEV RKASVHYKPL RGISDRHIHD LVRSIAACET
GAAANLAVKK ATNAFLELKE VRGYRGRLSP LAYEEFQRHT VRYLTIYKAS CGFEINVSMR
YKCRSNRGES CVISRVRYNR GDEIVGLSGC LAKMTKDEEL ALANDFSVLH SSRRGGNCLM
LGPARFVNHD CSANARFVPV PSGMVIQAVK PINVGDEITV KYAENYFGRR NKECLCQTCE
ENSRGLYGSP QESSEEESDD DMDELTKIEL QRRKKRQEQR EGGTPELREG GRGSSESSRE
TSEEAIEIST SKNWPLIPKI ESHTADSTPL PVPVGEVSEA TVTEVSTVVP AQEAIPVNES
TTALSQSSNE FQDPTIDPIL NGASAEIRFP SLPSPDTTTS PESQVPPFIQ PKSARRNHHY
LGMHNTDERV RFNDRLSVLD ERGGSEDMES CLVSGSESRD DSTAMSRDEE SSRDDGDGSR
SKRSKRHVRA QRKNSGSWSF SQEDLSFDRL CKAAREQAYD PSRYALTGVY GFSVSGATQT
CVSCCSVYNL TDGPKTLGHF CPRCHRHAAI HSFAWPYTNH KHALPLCLLM MRPPKKLEDE
DWGLSKPQVA QQFGAKNRKI FEEDGSLVQK KRKSLAWSWE YTKEEPAQEI TSMRIEDMSP
KELKKWSQAG RQTRSGRVSM LPEKPKRSRK SAPEPVEMRD NVAQLSREER AWKRARRGTV
GHEKVEVNTP TVETPSTGTP KVKKLHWKQK LAMERRQKEA EAAEVAETRV ADGVDASTPS
PAGSTPTPRG RGRPRKSSRE EEIPPEKTPE AKRPSPAATK TPSMSPKVKK EPLSMSFSMS
PTSRSGRVRN PTEKALQLME QGEYVI
