ID   SET9_PHANO              Reviewed;         662 AA.
AC   Q0U3A4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=SNOG_13760;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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   -!- SEQUENCE CAUTION:
CC       Sequence=EAT78784.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445352; EAT78784.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001803966.1; XM_001803914.1.
DR   AlphaFoldDB; Q0U3A4; -.
DR   SMR; Q0U3A4; -.
DR   STRING; 13684.SNOT_13760; -.
DR   GeneID; 5980888; -.
DR   KEGG; pno:SNOG_13760; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   InParanoid; Q0U3A4; -.
DR   OMA; FANHDCG; -.
DR   OrthoDB; 953612at2759; -.
DR   Proteomes; UP000001055; 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..662
FT                   /note="Histone-lysine N-methyltransferase SET9"
FT                   /id="PRO_0000281806"
FT   DOMAIN          114..228
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          252..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   662 AA;  75177 MW;  030125F3547BBF0E CRC64;
     MPPSKAEKRG LTLEKLASYD DVITDALVDK IYYWATIRKN RGTRFTASRG LQEEDIAGVI
     REQVIWDKDP VEAVQQLLDL PGLRKYMKGL RDEKDQDQFK RHLRRYVNIY MPDCPFEVTT
     TNRYTITDHE ASITARRDIN PREEIKYLTG VQVAMTEEQE KTLELARKDF SLVISSRKKT
     RSLFLGPARF ANHDCDANAR LSTKGYDGMQ IVAVKPINEG DEITVSYGDD YFGDNNEECL
     CHTCEDRQQN GWAPMKRVED SDDEDMEEAE SPVENPSEAT SSGTATSGGK RARDITEEDA
     GADLPPTSKR ARIEKKPSPT KARASDHLRE ATLKKVHSTS SLRREMPVSS IEDPSANINV
     TSPQMTQDIR NQQRDGLLTV SLDETSSSRE STPQSPLMAA SPKSSHSTDA TSVDDEHHVD
     SLPKIKVEPE VVHENPALGV ATVKEEVITT TVNAPWPSPP AEDDEMSDLS ELSDSMEFDS
     VKQQIVKRKF RPTLRTTRSK SRYEVHNRVG TPVSSAVGQD GEWVENPRKP GDYMTSSSLL
     SAKFSKWVEC QTCDVQFVQQ DGYNTRKECP RCERHSKLYG YAWPKTEREG KHDKEERITD
     HRIVHRFVDP DEERELKRGK TKKILKESIR ERFSTPRSGR ESMSASVEVD SGRKRRRVRK
     TM