ID   SET9_ASPFU              Reviewed;         622 AA.
AC   Q4X1W8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=AFUA_2G08510;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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}.
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; AAHF01000001; EAL93147.1; -; Genomic_DNA.
DR   RefSeq; XP_755185.1; XM_750092.1.
DR   AlphaFoldDB; Q4X1W8; -.
DR   SMR; Q4X1W8; -.
DR   STRING; 746128.CADAFUBP00002388; -.
DR   EnsemblFungi; EAL93147; EAL93147; AFUA_2G08510.
DR   GeneID; 3513303; -.
DR   KEGG; afm:AFUA_2G08510; -.
DR   VEuPathDB; FungiDB:Afu2g08510; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   HOGENOM; CLU_013724_0_0_1; -.
DR   InParanoid; Q4X1W8; -.
DR   OMA; FANHDCG; -.
DR   OrthoDB; 953612at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
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; 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..622
FT                   /note="Histone-lysine N-methyltransferase set9"
FT                   /id="PRO_0000281798"
FT   DOMAIN          120..234
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          262..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  69939 MW;  6A46811359F7B0A4 CRC64;
     MPSAKKRDSP SVDRRDRLTL AKLASYDDIA TDALVDRAYF WTNTRKNRTK YNPMRGIVDD
     DVARVLLHDV IVAKDLAKAE RELLAMSGLK KFMARLPNNR EKDWFRRHLR KYIQMYLPDS
     PFEITTTNRY TITEYEAAVC ARKFIKQGQE IKYLSGTLVP MTREEERDLD LKRKDFSIVM
     SSRKKTPSFF LGPARFANHD CNANGKLVTR GSEGMQVVAT RDIYIGEEIT VSYGDDYFGI
     DNCECLCLTC ERLVRNGWAP HVPSEPQSKA STPALNDDTL STDSHVSSKK RKFAPDSDIE
     TSAPSTPCKR GKFVRQSSKL KSEVSFLEVA TSIEQPAGPS PVCNGSDMGA LGNSTVESDN
     DKAVDPALPS PPADSPPSTA ANESERSSTS TTATSVCDAA VKIKVEETIE QSAEKVSALS
     EANVELPTTS LRSGSTEGDT KLELSDQPST LKQGSIGSNR KERRKSRGKP LVVESVEAER
     QLVRVPGDYT KTSKLLAQTY DRWVDCHTCN AWFVQHDSYL TRRECPRCER HSMLYGYRWP
     KTDKEGPSDD EERVMDHRTV HRFLYPEEEA LISRKDRGVS FGVTPTPELS EPRTETEGSE
     GCEDRRTTRA SRRRTRSLRM TM