SET9_COCIM
ID SET9_COCIM Reviewed; 624 AA.
AC Q1E9C0; J3KI01;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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; ORFNames=CIMG_00843;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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}.
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DR EMBL; GG704911; EAS35489.3; -; Genomic_DNA.
DR RefSeq; XP_001247072.1; XM_001247071.2.
DR AlphaFoldDB; Q1E9C0; -.
DR SMR; Q1E9C0; -.
DR STRING; 246410.Q1E9C0; -.
DR EnsemblFungi; EAS35489; EAS35489; CIMG_00843.
DR GeneID; 4567810; -.
DR KEGG; cim:CIMG_00843; -.
DR VEuPathDB; FungiDB:CIMG_00843; -.
DR InParanoid; Q1E9C0; -.
DR OMA; FANHDCG; -.
DR OrthoDB; 953612at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034770; P:histone H4-K20 methylation; IEA:InterPro.
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; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; 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..624
FT /note="Histone-lysine N-methyltransferase SET9"
FT /id="PRO_0000281802"
FT DOMAIN 115..229
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 253..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 70340 MW; 0A2DAD3E2E3770E9 CRC64;
MAPTPPPKQK GKLTLAQLAA YDDIVTDALV DRAFFWTKIR KNRPKYFAVR GVVEDDVTSI
LLHDVIVAKD VIKAEKSLLN LSGLRKYVET LKSDKEKEWF RRHLRKYIAI YLPDCPFEVT
TTNRYTITTH EAALSARKFI RTGDTIKHLS GTLVAITPEE EKTLDLTRRD FSIVMSSRKK
TPSLFLGPAR FSNHDCNPNA RLVTKGSEGM EIVAIRDISI GEEITVSYGE NYFGVDNCEC
LCHTCELSLS NGWSPGGPPE HDSRASTPET TEHQEKSSSG SEKRKSPPES PSHPSEDMPS
KRPKFENILN LRLEISPPSS PDPIAEPLIT VNGGLRALRS HFASLAGKSD LRHFQKPHSN
FISASSSSDQ TSCSLCPDDE APTSTRSTSA TSISDSNVQV KTEPTVEQQP RASSETAPKT
ISGDHGLHVQ DIIRDNDESD LSDLSASWEI NDREMTAVKR EPVKKKKRKR KSSIIPTIEH
EAPKARTPGD YTKTPKLLAQ RYDRWVDCQT CNAWFVQGDA YLTRKECPRC ERHSKLYGYR
WPKTDREGRN DTEERVMDHR TIHRFLRTED EARVQRRGRG VSHATSPTPD VSENKTETDA
SEFGDERRLT RSLRRARSSL RLAI
