ID   SET9_ASPTN              Reviewed;         629 AA.
AC   Q0C9E6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ATEG_09688;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476608; EAU29879.1; -; Genomic_DNA.
DR   RefSeq; XP_001218310.1; XM_001218309.1.
DR   AlphaFoldDB; Q0C9E6; -.
DR   SMR; Q0C9E6; -.
DR   STRING; 341663.Q0C9E6; -.
DR   PRIDE; Q0C9E6; -.
DR   EnsemblFungi; EAU29879; EAU29879; ATEG_09688.
DR   GeneID; 4354340; -.
DR   VEuPathDB; FungiDB:ATEG_09688; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   HOGENOM; CLU_013724_0_0_1; -.
DR   OMA; FANHDCG; -.
DR   OrthoDB; 953612at2759; -.
DR   Proteomes; UP000007963; 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..629
FT                   /note="Histone-lysine N-methyltransferase set9"
FT                   /id="PRO_0000281800"
FT   DOMAIN          120..234
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          264..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  71319 MW;  2D085F90ED32A649 CRC64;
     MAPSKARSSP AVERRDRLTL AKLASYDDVA TDALVDRAYF WTNTRKNRTK YIPVRGIMDD
     KVAEILLHHV IVAKDTVKAE RELLAISGIK KYMAKLPSDR EKEWFRRHLR KYIQMYLPDC
     PFEVTTTNRY TITEHEAAIC ARKFIKQGQE IKYLSGTLVP MTREEEQDLD LKRKDFSIVM
     SSRRKTPSFF LGPARFANHD CDANGRLVTR GSEGMQVVAT RDIEIGEEIT VSYGEDYFGI
     DNCECLCLTC ERAVRNGWAP QVDSEASSTA STPALNDETK SAHGSTSPQK RKYAPDADSD
     ASASPTPQKR RKFSRQYSKL RTEVSLSGDV TAIEPDPEQN TKIAVETTTD VPKDKPATNG
     VTENESNARV SENQRATSDR EPSSPLGVDE SQNSSASTAP TSLFDVGIKL EESTEAFTQE
     TLTTTKAGSV ADSHGDGDCR QLTAGIEQEA LSELSESLEL DDKSGTVVKR RKRRTRRQVV
     PSVEDESHRV RVPGDYTKTS KLLAQSYDRW VECRTCKTWF LQHNSYLTRR ECPRCERHSM
     LYGFQWPKTD KDGPLDDEER VMDHRTVHRF LYPEEEARIS RRDRGVSFGV TPTPELSEPR
     TETEDSEACD ERRNTRASRR RTQSLRMTM