ID   F9XEZ7_ZYMTI            Unreviewed;      1163 AA.
AC   F9XEZ7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
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};
DE   Flags: Fragment;
GN   Name=SDG2403 {ECO:0000313|EMBL:EGP85597.1};
GN   ORFNames=MYCGRDRAFT_10108 {ECO:0000313|EMBL:EGP85597.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP85597.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP85597.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
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; CM001202; EGP85597.1; -; Genomic_DNA.
DR   RefSeq; XP_003850621.1; XM_003850573.1.
DR   AlphaFoldDB; F9XEZ7; -.
DR   STRING; 336722.F9XEZ7; -.
DR   EnsemblFungi; Mycgr3T10108; Mycgr3P10108; Mycgr3G10108.
DR   GeneID; 13401081; -.
DR   KEGG; ztr:MYCGRDRAFT_10108; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_1_0_1; -.
DR   InParanoid; F9XEZ7; -.
DR   OMA; CHMTALF; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000008062; Chromosome 7.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_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; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS51572; SAM_MT43_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EGP85597.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGP85597.1}.
FT   DOMAIN          150..238
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1021..1138
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1147..1163
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          759..793
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..288
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..663
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGP85597.1"
FT   NON_TER         1163
FT                   /evidence="ECO:0000313|EMBL:EGP85597.1"
SQ   SEQUENCE   1163 AA;  130706 MW;  F53A5CE470340A25 CRC64;
     LTPLTSHSDS SPPKVSTPQH AHMSATDPTG ASATTHVPTS TDAPQRERAP RPQMMPPPGK
     VKGYRAVWDP ELDNKLSKEE RKRATFRKKD FGAETYEPDP PPDPRLAIPG YMSGQCRQKT
     TPSKAILRPA PYTLPPYKVD RYSIGPGEPQ QVVAVGFDPF LSESTLKLNF GTFGSIASVQ
     NKTDPETGSF LGIALIKYRD SIRDGEEISA VNAAKRAEVE FNGARIGVHT IKVELDREGR
     RCKRHVDHVL KKAKEERAKY APQPPGPPET PTDAKDSPAP PPNAPKGPSA KPAGKAAAAK
     AAGKPVRGVP GAATATPAPE TAANPKTGAA ALVEDEPILS KIKRKPYIHI PHASVPVLGT
     TIPHLKKRLK AYDWREVRLD VTGYYVIFED SKRGEDETER CYNECNKQAL FTYKMGMECQ
     KYGNPDYERS PSPERAMAEK QKQEEFERLQ KEDAEDLEIE KKSRAENLDP VLGALDQLRI
     ELRDRILGDI KTRIAIPIFH DSLDPTRHVA KRRKLGLPDP SDKENKGSSL LFAKAGDAPP
     DTPKNRRGYP LSHSKKPLRP HDPHNQRGRK GGREREPSNA FVDERRRKPP PRPTHARGLH
     FRLQQMYAEE EDSDDERQTS VTGRDTDEQE SRPLSRASRN STPFDSESVM DTPKHKRRKV
     TDWEDDEKET FEAFHKEMLG HLLHKEPEDL ATRELELVVN TLPRSSRYAT RARTELFIRQ
     RSKADDDLFQ VRLDRKDVDE ESVLASKEQA DTPAVELDAK VVKEKAKRKR KTKKQLLEEQ
     EALKAEAKKA KEESKPIAAA ETVTKIEQKE LEIEAVVEAE AQDKDVSLHL TFDKPRRTVE
     EDRSIILDID GWQQFIKDEE DMAFARKALA EQPAYDIGDV KLWAWKQKEI KALNSGGIPG
     QAQPEPLISG YYVPNPTGCA RTEGFKKILN EEKSKYLPHR IKVQRAREER QAQATSNPTA
     AAEAAKIKEA EKIASTATSR SNRVNNRRLV NDINLQKQTL ATANSDADVA IRFNQLKKRK
     KLVKFDRSAI HGWGLYAEEN IAVNDLIIEY VGEKVRQKIA DLREIRYEKQ GVGSSYLFRM
     IDDEIVDATK KGGIARFINH SCSPNCTAKI IKVEGTPRIV IYALKDIGKN DELTYDYKFE
     REMDSTDRIP CLCGSANCKG FLN
//