ID W7M9U7_GIBM7 Unreviewed; 940 AA.
AC W7M9U7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839, ECO:0000256|PIRNR:PIRNR037104};
DE EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182, ECO:0000256|PIRNR:PIRNR037104};
GN ORFNames=FVEG_07811 {ECO:0000313|EMBL:EWG47786.1};
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:EWG47786.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG47786.1, 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: Catalytic component of the COMPASS (Set1C) complex that
CC specifically mono-, di- and trimethylates histone H3 to form
CC H3K4me1/2/3, which subsequently plays a role in telomere length
CC maintenance and transcription elongation regulation.
CC {ECO:0000256|PIRNR:PIRNR037104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000256|ARBA:ARBA00000944,
CC ECO:0000256|PIRNR:PIRNR037104};
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC {ECO:0000256|PIRNR:PIRNR037104}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037104}.
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DR EMBL; DS022251; EWG47786.1; -; Genomic_DNA.
DR RefSeq; XP_018753977.1; XM_018896498.1.
DR AlphaFoldDB; W7M9U7; -.
DR GeneID; 30065583; -.
DR VEuPathDB; FungiDB:FVEG_07811; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd20072; SET_SET1; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR017111; Set1_fungi.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF11767; SET_assoc; 1.
DR PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 2.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037104};
KW Chromosome {ECO:0000256|PIRNR:PIRNR037104};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037104}; Nucleus {ECO:0000256|PIRNR:PIRNR037104};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR037104};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037104}.
FT DOMAIN 798..915
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 924..940
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 85..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 106390 MW; A26F0E26810B3D36 CRC64;
MHPETGSYLG FATIRYRDSK RTDRPPVSAM EAARRAVRTR GIKVDADIVR VEYDAEGRRS
RRMLEEHLKR EKEKFEKKEQ ERLALAAKAP PTGPKSGTAP VFTRPPPTAP KGPSAQRQPV
VPSAPQLSLT PSQQKGLNLE SSNLTQKLAD DPYIYVTGDS VPVLPSILPH MKKRLKNYGF
EEIRVDKSGY FIVFRNSFTG KSEAERCFRA VNHTEFFNYD MTMQLCLPRP HRDGPSSHRR
SSASPERKTN PEPRYRDEKE RRRREEEADL EEEKKQRAKN FDPVIEAVEV VRREMTEHLI
RHIRTKVAAP ALSDFLDPAN HAAKRRKLNI EHPDDLQEMA SVEDGNDSSR VGTPNSRADP
IERPTGRIAP KALPRIRKTK VKQKNAFVDP FARKRPPVAR NPFRSLHHRL RGLDSDAESD
DDTDTRTLLA RETEEAESRP RSRMSTDDEA SKDDFVPWEQ GEDDSMTEAS FAIADSAHSR
KRKLAESVES AFKRQKKSDE ELFGVRLTAL GSGFETREGS ADIIPELETG DDIDSRISRS
ETPVSVVGKP LKKRPSRAKK PKIFEDLGAQ DLRAETESQR DEEEAVEPPK ANAKKAVAIT
EKPTAKEVVT EKYDEKLLST EPLTPALALP DGAKPDLPLF QGLAIGQSDI PDVSKLSRRF
TAKDIGNPEL WLWTRNRIRE LNSANRTLDS PVTIGGYYVP NPTGCARTEG VKKILNSEKS
KYLPHHIKVQ KARQELEARN KSGKDAARIA IEKQAATDSE RNKRASNRRY VQDLNDQKKT
LGQDADIFKF NQLKKRKKPV KFERSAIHNW GLYAMENIAK DDMIIEYVGE QVRQQIAEIR
ENRYLKSGIG SSYLFRIDDN TVIDATKKGG IARFINHSCD PNCTAKIIKV EGSKRIVIYA
LKDIATTDEL TYDYKFEREI GSLDRIPCLC GTANCKGFLN
//
