ID   SET9_SCHPO              Reviewed;         441 AA.
AC   Q9USK2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Histone-lysine N-methyltransferase set9;
DE            EC=2.1.1.372 {ECO:0000269|PubMed:15550243};
DE   AltName: Full=Lysine N-methyltransferase 5;
DE   AltName: Full=SET domain protein 9;
GN   Name=set9; Synonyms=kmt5; ORFNames=SPCC4B3.12;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-220.
RX   PubMed=15550243; DOI=10.1016/j.cell.2004.11.009;
RA   Sanders S.L., Portoso M., Mata J., Baehler J., Allshire R.C.,
RA   Kouzarides T.;
RT   "Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites
RT   of DNA damage.";
RL   Cell 119:603-614(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDP1,
RP   HISTONE-BINDING, AND FUNCTION.
RX   PubMed=19250904; DOI=10.1016/j.molcel.2009.02.002;
RA   Wang Y., Reddy B., Thompson J., Wang H., Noma K., Yates J.R. III, Jia S.;
RT   "Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein.";
RL   Mol. Cell 33:428-437(2009).
CC   -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC       'Lys-20' of histone H4 to form H4K20me3. H4 'Lys-20' methylation is
CC       apparently not involved in the regulation of gene expression or
CC       heterochromatin function but participates in DNA damage response by
CC       giving a 'histone mark' required for the recruitment of the checkpoint
CC       protein Crb2 to sites of DNA damage. {ECO:0000269|PubMed:15550243,
CC       ECO:0000269|PubMed:19250904}.
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:0000255|PROSITE-ProRule:PRU00900,
CC         ECO:0000269|PubMed:15550243};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
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; CU329672; CAB60686.1; -; Genomic_DNA.
DR   PIR; T50436; T50436.
DR   RefSeq; NP_588078.1; NM_001023070.2.
DR   AlphaFoldDB; Q9USK2; -.
DR   SMR; Q9USK2; -.
DR   BioGRID; 276106; 26.
DR   STRING; 4896.SPCC4B3.12.1; -.
DR   MaxQB; Q9USK2; -.
DR   PaxDb; Q9USK2; -.
DR   EnsemblFungi; SPCC4B3.12.1; SPCC4B3.12.1:pep; SPCC4B3.12.
DR   GeneID; 2539545; -.
DR   KEGG; spo:SPCC4B3.12; -.
DR   PomBase; SPCC4B3.12; set9.
DR   VEuPathDB; FungiDB:SPCC4B3.12; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   HOGENOM; CLU_013724_0_0_1; -.
DR   InParanoid; Q9USK2; -.
DR   OMA; KFEICST; -.
DR   PhylomeDB; Q9USK2; -.
DR   BRENDA; 2.1.1.372; 5613.
DR   Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q9USK2; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0000785; C:chromatin; IC:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IMP:PomBase.
DR   GO; GO:0031491; F:nucleosome binding; IPI:PomBase.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IBA:GO_Central.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:PomBase.
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   1: Evidence at protein level;
KW   Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..441
FT                   /note="Histone-lysine N-methyltransferase set9"
FT                   /id="PRO_0000281807"
FT   DOMAIN          108..221
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   MUTAGEN         220
FT                   /note="Y->A: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:15550243"
SQ   SEQUENCE   441 AA;  51014 MW;  553FC8E19FFF42B3 CRC64;
     MRQTNTHLET FSLFDDVCTC LLVDKVFYWS QIHKVRKLVD RSIERMESCS IINIITKYII
     EQTDLDQAAK NILQFRELDP LLRRLSSTSL LAFTRHLKYY LSLYLPSCKF EICSTNQYFS
     SSKPEACVIA RESINAGEDI TDLCGTIIKL SPKEERNIGI GKDFSILHSS RLDSMCLFLG
     PARFVNHDCN ANCRFNTSGK RIWLRCVRDI KPGEEITTFY SSNYFGLENC ECLCVSCERM
     GINGFKKLFH TSATSTSCSS KSSSDVSDLS SLPQSNRYVI SEEDRSFLNI WDSGGELSDA
     SSSDLDEEFS LFIPRHKKRV WSREKRLLSE MAITNHSPLL NVDDYRKFRE DLWKKRHGKR
     KVYQCSNCSQ TFINEDIQNS SAFCPKCIRH SKLFSLPWPC RHKVNRELKL EKEKEINTKR
     NLVTSSHSMS LRHKKAVDYQ S