ID   SET9_EMENI              Reviewed;         641 AA.
AC   Q5AZY3; C8V2A8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=AN6147;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000105; EAA57933.1; -; Genomic_DNA.
DR   EMBL; BN001301; CBF70089.1; -; Genomic_DNA.
DR   RefSeq; XP_663751.1; XM_658659.1.
DR   AlphaFoldDB; Q5AZY3; -.
DR   SMR; Q5AZY3; -.
DR   STRING; 162425.CADANIAP00006863; -.
DR   EnsemblFungi; CBF70089; CBF70089; ANIA_06147.
DR   EnsemblFungi; EAA57933; EAA57933; AN6147.2.
DR   GeneID; 2870879; -.
DR   KEGG; ani:AN6147.2; -.
DR   VEuPathDB; FungiDB:AN6147; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   HOGENOM; CLU_013724_0_0_1; -.
DR   InParanoid; Q5AZY3; -.
DR   OMA; FANHDCG; -.
DR   OrthoDB; 953612at2759; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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..641
FT                   /note="Histone-lysine N-methyltransferase set9"
FT                   /id="PRO_0000281803"
FT   DOMAIN          120..234
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          261..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  71748 MW;  284DAF46C27C6F59 CRC64;
     MPSSKARSSP SVDRRERLTL AKLASYDDVA TDALVDCAYF WTKTRKNRTK YIPVRGLAED
     TVAHILLHDV IVAKDVSAAE RKILDLIGMK RYLAKLPNDR EKDWFRKHLR KYIQMYLPDC
     PFEVTTTNRY TITEHEAAIC ARKFIPQGQE IKYLSGTLVP MTKEEERDLD LKRKDFSIVM
     SSRRKTPSFF LGPARFANHD CSANGRLVTR GSEGMQVVAT RDIYIGEEIT VSYGEDYFGI
     DNCECLCLSC ERVPRNGWSQ NLAPGPQSKP STPEPKASED HLTPRKRKAQ SDIDSDSSPS
     STPRKRGKFT PRGSKLRSQL SLTEDIAISI ESEPRVPSSN LALSAQEAGD SGKSSSAGDN
     VESSGTDSES LTSITPQESQ RSSASTAATS VFDEAVSLNT RPTKSAVTTA APAESSIAAE
     APLSTTIPET DIKLEVEPSC EPTTTVTAQL DTTVRADSCV SDISSSTKLE DGSEALEHVK
     KPRKPRTKRV YLTIEPESKL NRVPGDYTKT PKLLAHSYDR WVDCHTCNAW FVQQNSYLTR
     RECPRCERHS MLYGFRWPKT EKEGPNDDEE RVMDHRTIHR FLYPEEEALV SRRGRGVSFG
     LTPTPELSDM RSETPDSEAL DERGNTRVTR RRTRAIRVTT V