ID A0A0D2GH31_9EURO Unreviewed; 787 AA.
AC A0A0D2GH31;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=Z517_06708 {ECO:0000313|EMBL:KIW80093.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW80093.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW80093.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW80093.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846972; KIW80093.1; -; Genomic_DNA.
DR RefSeq; XP_013283901.1; XM_013428447.1.
DR AlphaFoldDB; A0A0D2GH31; -.
DR STRING; 1442368.A0A0D2GH31; -.
DR GeneID; 25306198; -.
DR VEuPathDB; FungiDB:Z517_06708; -.
DR HOGENOM; CLU_013724_0_0_1; -.
DR OrthoDB; 1705992at2759; -.
DR Proteomes; UP000053029; 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:UP000053029};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 118..232
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 259..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 86885 MW; 47CBDB95CD4CC1A2 CRC64;
MARGKGAAEP EKSQRLSLAE LAAHDDVCSD VMIDNAYYKA RIRKNRTKHI PIRGIKEDEV
PQILLHKVIV DKDVDAAEKA LLALPGLKRY RKSLRSKTEQ EHFLRHLRKY IEMYQTDCAW
EVSTTNRYTI TTYEAAVTAR RRIRQGDTIK YLTGTLVPLT TEESADLDLT NRNFSIVVSS
RKKNSSIFLG PARFANHDCD ANGRLVTRGE NGMEVVAMKN IEVGDEITVS YGDDYFGPGN
IDCLCHTCEQ LERNGWTSKA GILDTPSRTS TPVHEPQSVV QSRGLKRKRD SNPSQSSSVP
PPSKHAKGVQ SPSKLQHSWT PSDSSDAETP LLPVERNSEP IEDLRTLASE TGAALSPPRS
PLQPETHGSG EFLTPVGIES SAPENGVDHG SEQSPGLSQT YTNSSASRKN ANLLGKICSR
APLSPAPTSP SSHGSATEAG QSRIPIPKPY NADTVVTVKV ETVQTTKVEE DEEEAYYDDE
DTVVMIESKP ESAQTTGSLR QSQERPKRPS TITENNSSVI PHTVSILSTT TVSKEVRPVE
SPVAAATETS VLPSIEPVTV STTVSTLTVH PVTGTIRIAG DYILTRKLLA QPHDRWVQCH
NDKCLGFFIQ PNGYQTRREC PRCERHSMLY GFPWPKTDPD PRKLLERRSQ GTGRGKKNNA
PATEYSAYRR KGRCGKGTWV EGGGDPEERV MDHRTIHRFV LPEEERELTR KGLLKEAEIA
RAAGDHALAI LEARMRANSS SRALNHGTAT ESATRDVSES GSATPDELRR RSNRFVTRPV
GVYTDKF
//
