ID W7MAT4_GIBM7 Unreviewed; 668 AA.
AC W7MAT4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=FVEG_05617 {ECO:0000313|EMBL:EWG44599.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG44599.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG44599.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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; DS022247; EWG44599.1; -; Genomic_DNA.
DR RefSeq; XP_018750790.1; XM_018893862.1.
DR AlphaFoldDB; W7MAT4; -.
DR STRING; 334819.W7MAT4; -.
DR EnsemblFungi; FVEG_05617T0; FVEG_05617T0; FVEG_05617.
DR GeneID; 30063598; -.
DR KEGG; fvr:FVEG_05617; -.
DR VEuPathDB; FungiDB:FVEG_05617; -.
DR eggNOG; KOG2589; Eukaryota.
DR HOGENOM; CLU_013724_0_0_1; -.
DR OMA; FANHDCG; -.
DR OrthoDB; 1705992at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
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:EWG44599.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EWG44599.1}.
FT DOMAIN 116..230
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 261..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 75371 MW; C2066089F6B816E7 CRC64;
MPPSQKAAAK KPRMTLAQVS AYDDILTDAL VDHVFYWTTV PKNRTSYHPS RGVREEEIAK
ILQEEVVLKK DLDSAEKRLL TTNGLKRFHN GLKTDNEKEN FRRHLRRYVQ IYLPDCPWEV
SSTNRYTIVT HEAAVTARRP IRRNEAIKYL SGVQVIITPE EEKAISSQKK DFSIVVSSRS
KCTSLFMGPA RFANHDCDAN AKLMRTSHAG IEIVATRPIE AGEEITVTYG DNYFGENNCE
CLCKTCEDLL QNAWEPEEGT VPVKTSIEQE KSEGYSLRRR RRDDSISGSS RTPSVTPDMR
PRITKATSRG SKLARDSSSA RSPPAEQSNN RKRQHESLAT PPKTPAKRQK VSAEKTVLII
DDSSRSTSVT ASESSSGVVE TDVTSPEKET PEPLGHTPLK GIANKGSQQR EGAPVSPQSS
QGSQSPQQAA EMARERTRRS GLESMTIQAI LNAPIESEVE SEPEPEKLKE ATVVPPPTEP
IATSIETVED SQVADEDQPK RKKYQRRVYK EDTPPSRVRV PGDYLLTPLL LSEPEMAWIQ
CTICDGYFVQ QNAYFTRASC PRCERHSKLY GYIWPKTDKA GPHDKEERIL DHRTIHRFLD
PDDERKVRCR KSFGNLKTDT EETEELERGR KRHSTSGLMG RTGPSSEQDS NHRRSGRLRR
VNSRFLDP
//
