ID   C9SDJ7_VERA1            Unreviewed;       494 AA.
AC   C9SDJ7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=VDBG_02527 {ECO:0000313|EMBL:EEY16418.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(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}.
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DR   EMBL; DS985216; EEY16418.1; -; Genomic_DNA.
DR   RefSeq; XP_003006388.1; XM_003006342.1.
DR   AlphaFoldDB; C9SDJ7; -.
DR   STRING; 526221.C9SDJ7; -.
DR   GeneID; 9535437; -.
DR   KEGG; val:VDBG_02527; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   HOGENOM; CLU_013724_0_0_1; -.
DR   OrthoDB; 1705992at2759; -.
DR   Proteomes; UP000008698; 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:EEY16418.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEY16418.1}.
FT   DOMAIN          116..230
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          280..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  54848 MW;  52731F19A819492B CRC64;
     MPPSKALSAR KQALTLTQLA TYDDILTDAI VDHVFYWTTI PKNRSSYHAS RGVREEEIAK
     IIQTDLVLNK DIDAAERNLL TTDGLRKFCN SLKTDKEKAD FRGHLRRYLN LYLPDCPFEV
     NSTNRYTIVS HEAAITARRF IARNETVKYL SGVQVMITPE EEREMTARKK DFSIIISSRN
     KCASLFMGPA RFANHDCKAN AKLVTTGQAG IEIIATTNID VGDEITVTYA DSYFGEDNCE
     CLCSTCERRQ ANGWHNEEDT TVKRSIEDHS AEGYLLRRRR RDDSVDRTSR TPSVSADIRP
     RVSKSRRGRK SDHNPSVNDS AAAESPLPPA ATKKRTLNTL TPPITPAKKS KLSSNNAIPA
     PIEPESSRSS SAGSPRSHSL SSTDHGASTD ITEPERQSPE RHLLKPLVVR KDDFSLLKRE
     ETDERSSTTL TQISLFSSPA NITVTTQSDR PLDDTPPSTR PLSIASLCNP PSPPSSQELA
     NTTNHAISAP QRSQ
//