ID A0A1Q5UEQ9_9EURO Unreviewed; 706 AA.
AC A0A1Q5UEQ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=PENSUB_3769 {ECO:0000313|EMBL:OKP10949.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP10949.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP10949.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP10949.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OKP10949.1}.
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DR EMBL; MNBE01000310; OKP10949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5UEQ9; -.
DR STRING; 1316194.A0A1Q5UEQ9; -.
DR OrthoDB; 1705992at2759; -.
DR Proteomes; UP000186955; 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 ECO:0000313|EMBL:OKP10949.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OKP10949.1}.
FT DOMAIN 141..255
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 281..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 79639 MW; CB31EC6B648F90DD CRC64;
MPPKKARSSS PATERRERLT LAKLASYDDV ATDALVDHVR LQLTFGTQSH DTDHFFLQAY
FWTTTRKNRN KYGPARGIHD DDVGHILLHD VVVAKDIPTA ERKLLELPGL RKYQANLPSP
REKEWFRRHL RKYIQMYHPD CPFEVTTTNR YIITQHEAAI CARKFIKAGQ EIKYLAGTLV
AMTKEEEMDL GLTRKDFSVV MSSRRKTPSF FLGPARFANH DCDANGRLVT RGTEGMSVMA
TRDIHEGEEI TVSYGEDYFG IDNCECLCMT CEHSVRNGWS PQVESDENDE ETSPILLDED
GPGDHKSGSK KRRRDSDPDT EDLSSVCSTP NKRAKFHRQT SKLREEICMA DLTAQSTTTP
ESYNPLTPES DLDTSVLPIS VAGDRQVSKL RQEIIVTEGV QSPPETLVPS TQETNQTNQS
QSKTDIAVID TDAVTLIDPT TITNPAADGP ADCHSPSSTD ESRQSSSSSL PTSVDETGIK
VKTEESAESS RLDPSQETII GEGRPDTPIT GQPETPISLP RSPTLSEILG LSHSFEPDDA
QTLGEKKRKP RRKRNWAIVA SVETEVPVTR SPGDYTKTSR LLAQKYDRWV DCQTCESWFV
QSNSYQTRRE CPRCERHSKI YGFQWPKTEK GADREERVMD HRTIHRFLSP DSEARVSRRD
RGISFGVTPT PELSDARTET PTSDANEPRR NTRASRRRTR DLRMTM
//
