ID G9NC38_HYPVG Unreviewed; 681 AA.
AC G9NC38;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=TRIVIDRAFT_38211 {ECO:0000313|EMBL:EHK15263.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK15263.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK15263.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK15263.1}.
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DR EMBL; ABDF02000092; EHK15263.1; -; Genomic_DNA.
DR RefSeq; XP_013949466.1; XM_014093991.1.
DR AlphaFoldDB; G9NC38; -.
DR STRING; 413071.G9NC38; -.
DR EnsemblFungi; EHK15263; EHK15263; TRIVIDRAFT_38211.
DR GeneID; 25793692; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_38211; -.
DR eggNOG; KOG2589; Eukaryota.
DR HOGENOM; CLU_013724_0_0_1; -.
DR InParanoid; G9NC38; -.
DR OMA; FANHDCG; -.
DR OrthoDB; 1705992at2759; -.
DR Proteomes; UP000007115; 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:UP000007115};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 119..233
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 279..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 76859 MW; 66D949BA31556E65 CRC64;
MAPPKAAGAT AKKQRLTLSQ LAAYDDILTD ALVDHAFYWT TVPKNRSSYH PSRGIREGEV
AKIIQEDVVV NKDLEAAEKR LLTSVDGLKR YVNGLKLDKE KADFVQHLRR YLRIYMPDCP
WEVSTTNRYT IVTHEACVIA RRYIKRNETI KYLSGIQINI TPEEEKEITV RKKDFSIVVS
SRKKRTSLFM GPARFANHDC RANAKLMTTS QSTIEIVASR PIEVGEEITV TYSDCYFGDD
NCECLCRTCE KELRNGWAPG DEAVNVKISV EKDERKETYS LRRRRRDDSI GGSSRTSSVT
PDMRPRIYKT KPKVKKQDAQ DTSAIPTPAP EATPRGRKRT MDAMATPPIT PAKKLKLFAA
SSVDDSLSTR SVTPSHADAP ETDTASPEKE SPQPEAHTPP RFSAERLDTA KDEKQHAYKD
TINITVEPVS PQSMGSRASP DMVPVEAPVQ PLPRPRQLIT MSISSILNDP SAIEDPAEAY
YPFVANVRVA GQPVVESKFE LISEPEDAQT EQPKRRKRGT AIPKQSTPPP ARLRKPGDYV
LTPLLLSEPD MAWIQCTNCS DYFVQQNAYF TRSSCPRCER HSKLYGYAWP KTDKTGPSDK
EERILDHRMI HRFLDSNDER RARGRKLLSE TRDDTQEMDE ERGRASKRGP NRAGNTSQKD
GDSRVRRSGR ARRMSSKLIE G
//
