SET9_ASPOR
ID SET9_ASPOR Reviewed; 625 AA.
AC Q2TZH4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=AO090011000851;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007171; BAE65291.1; -; Genomic_DNA.
DR RefSeq; XP_001826424.2; XM_001826372.2.
DR AlphaFoldDB; Q2TZH4; -.
DR SMR; Q2TZH4; -.
DR STRING; 510516.Q2TZH4; -.
DR PRIDE; Q2TZH4; -.
DR EnsemblFungi; BAE65291; BAE65291; AO090011000851.
DR GeneID; 5998527; -.
DR KEGG; aor:AO090011000851; -.
DR VEuPathDB; FungiDB:AO090011000851; -.
DR HOGENOM; CLU_013724_0_0_1; -.
DR OMA; FANHDCG; -.
DR Proteomes; UP000006564; Chromosome 7.
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..625
FT /note="Histone-lysine N-methyltransferase set9"
FT /id="PRO_0000281799"
FT DOMAIN 120..234
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 260..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 70383 MW; ED6A776AF259BB94 CRC64;
MPSSKARDSP SVERRDRLTL AKLASYDDVA TDALVDRAYF WTNTRKNRTK YIPVRGVHED
DVARILLHEV IVAKDSAQAE KQLLAMSGMK KYLAKLPNDR EKEWFRRHLR KYIQMYLPDS
PFEVTTTNRY TITEHEAAIC ARKFIKQGQE IKYLSGTLVP MTREEEQELD LKRKDFSIVM
SSRRKTPSFF LGPARFANHD CNANGRLVTR GSEGMQVVAT RDIYIGEEIT VSYGDDYFGI
DNCECLCLTC ERAVRNGWAP HVDSEEGSSK ASTPALNDEA ISNDSLLSPR KRKHHLDSDS
DISPSSTPRK RSKFTRQSSK LRSAVSLADF APVGSGSDNP PPQAETSIVP ETTGAASITN
DTIVPASGSA VEVSQASATD CDSSPSLEAD ESHHSSTSTT PTSIGDVKIK VEDTVEASLT
ESASATHITL SITGQPHNDR HPPGTDNDML SELSEITDNP QKPKRSRGSR WKHGVVPSVE
EESHRVRVPG DYTKTSKLLA QAYDRWVDCH TCNVWFVQHN SYLTRRECPR CERHSMLYGF
RWPKTDKEGS MDDEERVMDH RTVHRFLYPE EEARISRKDR GVSFGVTPTP ELSEPRTETE
DSEACDDRRN TRASRTRTRS LRMTM
