ID   C7YTG9_FUSV7            Unreviewed;      1281 AA.
AC   C7YTG9;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839};
DE            EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
DE   AltName: Full=SET domain-containing protein 1 {ECO:0000256|ARBA:ARBA00030093};
GN   Name=SDG2101 {ECO:0000313|EMBL:EEU44617.1};
GN   ORFNames=NECHADRAFT_49470 {ECO:0000313|EMBL:EEU44617.1};
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122 {ECO:0000313|EMBL:EEU44617.1, ECO:0000313|Proteomes:UP000005206};
RN   [1] {ECO:0000313|EMBL:EEU44617.1, ECO:0000313|Proteomes:UP000005206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4
RC   {ECO:0000313|Proteomes:UP000005206};
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.J., Danchin E.G., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   Vanetten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
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|ARBA:ARBA00002789}.
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   -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC       {ECO:0000256|ARBA:ARBA00011755}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; GG698900; EEU44617.1; -; Genomic_DNA.
DR   RefSeq; XP_003050330.1; XM_003050284.1.
DR   STRING; 660122.C7YTG9; -.
DR   EnsemblFungi; NechaT49470; NechaP49470; NechaG49470.
DR   GeneID; 9665737; -.
DR   KEGG; nhe:NECHADRAFT_49470; -.
DR   VEuPathDB; FungiDB:NECHADRAFT_49470; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_0_0_1; -.
DR   InParanoid; C7YTG9; -.
DR   OMA; CHMTALF; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000005206; Unassembled WGS sequence.
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; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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   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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EEU44617.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005206};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1139..1256
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1265..1281
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1281 AA;  142018 MW;  82B0188A5F8DC822 CRC64;
     MTRPPGASFA QFFPTAPKVK AQAQSRADRD RDRDRPKTTS SSASINGGAS DPTPASAGFD
     AHANASAQPA PGPNGHLAVS DTLSAHPDDN GSPLADIPST VDSASSYSSA ASSIFSTSAR
     HGAAATATSS RLPTSSLTPI ASKDSPSNSS ATAPTKPDMS ASLAADRAAR QSSHNSPAVG
     PNGSISDGPL AIERPPARDP MPSVKGLKCT YDPLLDRVHN KSVSRNAKPT YKEFGRDDDA
     PPTDPRLSKP GGRLGYINTD YYLPKARLRP APENIKPYPY DPKTSIGPGP PTQIVVTRYN
     PLVPFSKVTA IFATFGEIAE SSNKMHPETG SYLGFATIRY RDSKRPDRPR VSAIDAARRA
     VRTRGIKVDA DVVRVDYDPE GRRSRRMLEE HLRREKERME KKEKERLAQA VQAPPIGPKS
     TPASNFTRPP PTAPKGPAAQ RPAGAPSTPQ PTTTPVQPKG HAAVEVKNLA SQLTDDPYIY
     IAGDSVPVLT SIVPHMKKRL KNYGFEDIRL DKSGYYIVFR NSFTGKSEAE RCFRAVNHTE
     FFNYDMTMQL CLPRPRRSDE SPERRRQASA SPDRKPRGET GQRDEKDRRR REEEADLEEE
     KKQRAKNFDP VIEAVEVVRR EMTEHLIRHI RTKVAAPFLS EFLDPANHVA KRRKLNIEHP
     DDIEEIPSIE DGNDSSRVGT PNSRADPIER RTGRLEPKAL PRIRKTKVKG QAQRSAFIDP
     FARQRPVARN AFRSLHHRLR SLDSDVESDD DTDTRALLAR ETEEPESRPR SRMSTDDEAS
     KDDFASWGPG EDDSMTEASF HITDPLISRK RKLDASVETA FKRQKKSDEE LFGVKLGQLG
     TGFVAREDSV DIIPEPETGD DLESRVSRSE TPASVIGKTL KKKPAKAKKK TKKAVFEERE
     ALKRQAETDS QRGDEDEVVE APKAEPKVEE KPPVAEPVPE PVVEKYDEKL LSTEPLTPAL
     VLPDGFKPDL SLFQGLALGV NDKPDVAKLS KRFAVKDIGD PELWLWKRNR IRELNSTKGT
     LEKPVSIEGY YVPNPTGCAR TEGVKKILNS EKSKYLPHHI KVQKARQERE ARFKKSGKDA
     AAAAAEAAKL AAEKLIAKGN SRANRATNRR YVADLNDQKK TLGQDSDVFK FNQLKKRKKP
     VKFARSAIHN WGLYAMENIA KDDMIIEYVG EEVRQQIAEI RENRYLKSGI GSSYLFRIDE
     NTVIDATKKG GIARFINHSC MPNCTAKIIK VEGSKRIVIY ALRDIAMNEE LTYDYKFERE
     IGSLDRIPCL CGTAACKGFL N
//