ID   Q0UWR1_PHANO            Unreviewed;      1168 AA.
AC   Q0UWR1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 117.
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=SNOG_03803 {ECO:0000313|EMBL:EAT89008.1};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT89008.1, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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, 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|ARBA:ARBA00011755, 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; CH445329; EAT89008.1; -; Genomic_DNA.
DR   RefSeq; XP_001794349.1; XM_001794297.1.
DR   AlphaFoldDB; Q0UWR1; -.
DR   STRING; 321614.Q0UWR1; -.
DR   EnsemblFungi; SNOT_03803; SNOT_03803; SNOG_03803.
DR   GeneID; 5971212; -.
DR   KEGG; pno:SNOG_03803; -.
DR   VEuPathDB; FungiDB:JI435_038030; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_1_0_1; -.
DR   InParanoid; Q0UWR1; -.
DR   OMA; CHMTALF; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
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; PF00076; RRM_1; 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   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:UP000001055};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1168 AA;  130831 MW;  7E8780CBF58846D8 CRC64;
     MSRSGQAISL SALTPLTTSS PSPRSAKTSY DTMNGTSSSR AAPSSAPENV ANTITPVNTP
     PETRKSVFPA DGVMAKRILY DPYSDAKLEK KVRHSKPAQY KTVLDKGDPS PPPDPRLALA
     GYTSGSYILK PTAKSKLRIA PYIAKPYAFD NRISCGPGPA TQVVVTGFDP LTPDSQLRGF
     FSTYGDVESL RAEVHPDNGS PLGICLIKFR DTPQARGSVA IKASTSAKRA EREGSNQRLG
     QQVIKVHTDR EGRRCAKLVE LVVQKSRKQE ENIRAKAAAK AAKASALATP ATFDLPANVP
     KGPSGRGARP PIPVPREPLN KKAALSHLIE KDPIKPKLKR APYLFIAHQY VPVLSTTIDH
     LKRRLKNFRW DALRCDQTGY YVVFASTKHG EDEAVRCFRE CHMKPLFTYV MNMECQQYGD
     PDYERSPSPE RVMADKKRKA IEDRMDQEES ADLELEKTQR AEAMDPVVAA LEQLKQELQE
     KILGDIKTRI AAPTLLELMQ PERHVEKRRR LNIAEPRKKE EDIRPPSLLV PGLDPFGAGT
     PKSRAAGFSG RGRKALGPYD RNRPGKKPPR IVNAFADERR KASAPKPRVA RGLHRQMIEM
     FEGPEESDDE SRSNLTRGTE EQESRPISRA PSTDVEEEEE ESSRAHRAKR RRIEAGWGED
     SDDEMMDDSH ARSLLAHCIH KDPENMAEKE LEQVLAILPR SSPIWKKADK ALKGFRRLRK
     IEQEADAIFG VETSPVDKLD PEVIVTQDDE PSKPIETTEL PETLKSLKKK QAAAKPKKKT
     KKQLEEEAKS AKAEVTEISL PEEDIAEVKE HALVPEVSVT EDTPEEDDTG SVMWGVSSTE
     PRKTVEDDFS VVMDIDGWQH MLKDEEDLLH LKAALQSIEA AKIGDAQSWA WKQKSIKHLN
     RPGGEEGVSR TETKIEGYYV PNPTGSARTE GVKKIRESEK SKYLPHRIRV QREREERQRQ
     AKKAEHAVIS VEGFKFTTSS QKASTANSRA NRANNRRMVN DINISKNMTG AEGDALRFNQ
     LKKRKKLVKF DRSAIHNWGL YAQENIVAND MIIEYVGEKV RQRVADLREV RYDQQGVGSS
     YLFRIDEDTV IDATKMGGIA RFINHSCTPN CTAKIIRVDN TKRIVIYALR DIGQDEELTY
     DYKFEREMDA TDRIPCLCGS VGCKGFLN
//