ID   A1CSR2_ASPCL            Unreviewed;       635 AA.
AC   A1CSR2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Histone-lysine N-methyltransferase SET9 {ECO:0000256|ARBA:ARBA00015413};
DE            EC=2.1.1.372 {ECO:0000256|ARBA:ARBA00024057};
DE   AltName: Full=Histone-lysine N-methyltransferase set9 {ECO:0000256|ARBA:ARBA00014232};
DE   AltName: Full=SET domain protein 9 {ECO:0000256|ARBA:ARBA00030653};
GN   ORFNames=ACLA_080330 {ECO:0000313|EMBL:EAW06349.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW06349.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW06349.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Histone methyltransferase that trimethylates 'Lys-20' of
CC       histone H4 to form H4K20me3. {ECO:0000256|ARBA:ARBA00001984}.
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:0000256|ARBA:ARBA00023940};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; DS027060; EAW06349.1; -; Genomic_DNA.
DR   RefSeq; XP_001267775.1; XM_001267774.1.
DR   AlphaFoldDB; A1CSR2; -.
DR   STRING; 344612.A1CSR2; -.
DR   EnsemblFungi; EAW06349; EAW06349; ACLA_080330.
DR   GeneID; 4700093; -.
DR   KEGG; act:ACLA_080330; -.
DR   VEuPathDB; FungiDB:ACLA_080330; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   HOGENOM; CLU_013724_0_0_1; -.
DR   OMA; FANHDCG; -.
DR   OrthoDB; 1705992at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140943; F:histone H4K20 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd10524; SET_Suv4-20-like; 1.
DR   Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1.
DR   Gene3D; 2.170.270.10; SET domain; 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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B-RELATED; 1.
DR   PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51567; SAM_MT43_SUVAR420_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          120..234
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          283..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..635
FT                   /note="Disordered"
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        318..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  72094 MW;  AB50A8B9373C83CD CRC64;
     MPSLKGRSSP AVERRDRLTL AKLASYDDVA TDALVDRAYF WTNTRKNRTK YIPIRGIVDD
     QVARILLHDV IVAKDASKAE RELLAMPGLK KFMGKLRNDR EKDWFRRHLR KYIQMYLPDS
     PFEITTTNRY TITEHEAAVC ARKFIKQGQE IKYLSGTLVP MTREEEQDLD LKRKDFSIVM
     SSRKRTPSFF LGPARFANHD CNANGKLVTR GSEGMQVVAT RDIYIGEEIT VSYGDDYFGI
     DNRECLCLTC ERLVRNGWSQ NAASELPGAA LIPAVNEDML TVDSHVSPKK RKSAPDSETE
     LSAPPTPSKR AKFIRQSSKL RSEVSFPEST NSIEQPAEQP SLINNAISNG PVAESVKNDP
     LDSNLDTTTV HTQPPSPDDY KSPSSITADE SQRTSTSTYV TSVCDTGLKI KVEQVIETSV
     EKVSSTIEKN IEFSTTSQPD LERRSTSSER DAQSELSDPP STMDLLETLV TETKKSRTSR
     RKNTIVSSVE VESQLVRVPG DYTKTSKLLA QTYDRWVDCH TCNTWFVQQN SYLTRRECPR
     CERHSMLYGY RWPKTDREGP QDEEERVMDH RTVHRFLYPE EESLVSRKAR GVSFGVTPTP
     ELSESRTETE GSDGGDDRRT TRASRRRTRS IRMTM
//