ID A0A0D2A2M1_9PEZI Unreviewed; 717 AA.
AC A0A0D2A2M1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=PV09_07802 {ECO:0000313|EMBL:KIW00605.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00605.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00605.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00605.1,
RC ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
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; KN847561; KIW00605.1; -; Genomic_DNA.
DR RefSeq; XP_016210474.1; XM_016361614.1.
DR AlphaFoldDB; A0A0D2A2M1; -.
DR STRING; 253628.A0A0D2A2M1; -.
DR GeneID; 27315775; -.
DR VEuPathDB; FungiDB:PV09_07802; -.
DR HOGENOM; CLU_013724_0_0_1; -.
DR InParanoid; A0A0D2A2M1; -.
DR OrthoDB; 1705992at2759; -.
DR Proteomes; UP000053259; 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:UP000053259};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 119..235
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 262..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 79819 MW; 7BF89C370F4293DA CRC64;
MAAQRDLGKA LAKKGGLTLA QLASYDDVLT DALVDRVYFW ATIRKNRPRF SPSRGIQEEE
VASILRDFVI VEKDPKRATD EILKLAGIRK YVDRLKTPDE REHFQRHLRK YVNIYLPDCP
FEVSTTNRYT IDTHEACVMA RKDIRKGEVI KYLSGIQVAI TEEEFKALSR DDVRLDFSIV
HSSRKKTPSL FLGPARFANH DCNANARLST TGSHGMQIIA TRDISVDEEI TVTYGTDYFG
EDNCECLCVT CERLRRNGWA VHAGSGKEDE ESEEKEQAED LEQEQKVSVA ENCDGQRKRK
SSALHEDDLL TGPSTPGSAS KRQKLTTPDR DTNSRQATPR GRRTVREVKV KSESTSAQQS
LRDLPAGAPQ AESHISMDVA ALPDLHQQSG CHTRTRSLRA SSGESGDSRS SSTAASSVFS
SRSQGTGVTS DGEIMDSIVV KVLGDDFIAV DAATTTASAA TTTQTCPTTV SVTTTAATRC
TTDINAEVTA TAGQEQNADE DLSDGELTTL SQFSVDESSG MAIRLSERLI KKRKKWNREL
AALREGSMER SLVEYLEEPA VAVLSTETDV SAGTDGPGRH PGDYTMTRRL LSGPYSRWVE
CQTCDAMFVQ EDAYLTRKEC PRCERHSKLY GFAWPKTERE GKWDTEERVL DHRTVHRFVE
PSEERKIKKG GRKSLQIEAL RARESLERTR SVSQTGTPAE GSPRRSGRRR ARSRLTR
//
