SET9_NEUCR
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 25-MAY-2022, entry version 101.
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}.
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DR EMBL; CM002238; EAA33797.2; -; Genomic_DNA.
DR RefSeq; XP_963033.2; XM_957940.2.
DR AlphaFoldDB; Q7SBJ9; -.
DR SMR; Q7SBJ9; -.
DR STRING; 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 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 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..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
