ID   SET9_NEUCR              Reviewed;         777 AA.
AC   Q7SBJ9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Histone-lysine N-methyltransferase set9;
DE            EC=2.1.1.372 {ECO:0000250|UniProtKB:Q9USK2};
DE   AltName: Full=Histone-lysine methyltransferase 1;
DE   AltName: Full=SET domain protein 9;
GN   Name=hlm-1; Synonyms=set9; ORFNames=NCU08551;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM002238; EAA33797.2; -; Genomic_DNA.
DR   RefSeq; XP_963033.2; XM_957940.2.
DR   AlphaFoldDB; Q7SBJ9; -.
DR   SMR; Q7SBJ9; -.
DR   STRING; 367110.Q7SBJ9; -.
DR   PaxDb; 5141-EFNCRP00000004675; -.
DR   EnsemblFungi; EAA33797; EAA33797; NCU08551.
DR   GeneID; 3879172; -.
DR   KEGG; ncr:NCU08551; -.
DR   VEuPathDB; FungiDB:NCU08551; -.
DR   HOGENOM; CLU_013724_0_0_1; -.
DR   InParanoid; Q7SBJ9; -.
DR   OrthoDB; 1705992at2759; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042799; F:histone H4K20 methyltransferase activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..777
FT                   /note="Histone-lysine N-methyltransferase set9"
FT                   /id="PRO_0000281805"
FT   DOMAIN          117..231
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          263..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  86094 MW;  F15745E5259F5AA0 CRC64;
     MTKPQGTGGK KKNQLTLAQL AAYDDILTDA LVDHAYYWTT IPKNRTSYHP SRGIKEEEIT
     KIIQNHLIVD PDIATAEEKL LATDGLKRFC NTLKTPREQN DFKAHLRRYM SIYLPDCPFE
     VNATNRYTIV TYEASITARR FIQRNETIKY LAGIQVVITP EEELEMSLRK KDFSLIVSSR
     SKSTSLFMGP ARFANHDCNA NARLITRGQA GIEIIACRNI EVGEEITVTY SESYFGENNC
     DCLCATCESN LRNGWRPVDG EAAVQKSIED EQPTESSTPY SFRRKRRYGS TALQASRTPS
     VTPDMRPRVL RKSQSQMMLG ERTSTTDSAA QGAGADGQSR KRALEMGTPP FTPTKKQKTT
     QYPVVPIALS TAPSRGSSDN ETSKSPLSFS TTNDNVTDAT SQGSESPGPI ILSPEPTPIK
     QAIGLLKQEE GVNEVAVQQV PEAFTPPPSQ PTEEEPPMVR PAFERLAARD RMSIANLISG
     PSSPAPPVVF SVAEVTTHRP KPQTLQLQKT DQTATISTLQ TVTAAVQKEA PVVKTESPIK
     PTVGQVEKIT QVQTTTKSCT PSKPKAQAAA LPQHHMPVST APRGRVPHDY TLTPLLLSEP
     ETAWIMCTHC ASAFVQKNAY LTKSTCPRCE RHSKLYGYMW PKTEKYGPND KEERILDHRM
     INRFLTAEEE ARARGRVYWR ERMGSKGKQG SSAPSTKGTP AGEKNEQSAK QEQSQGQYVQ
     ERFAVRKKVK VQVRSTVPTP VIMTKKDEVA EAAALGLRRS GRARRVSAKL ADCELDF
//