ID F7VTR0_SORMK Unreviewed; 1314 AA. AC F7VTR0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 24-JAN-2024, entry version 74. 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 ORFNames=SMAC_07534 {ECO:0000313|EMBL:CCC08898.1}; OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria. OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC08898.1, ECO:0000313|Proteomes:UP000001881}; RN [1] {ECO:0000313|EMBL:CCC08898.1, ECO:0000313|Proteomes:UP000001881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell RC {ECO:0000313|Proteomes:UP000001881}; RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC08898.1}; RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891; RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K., RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S., RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.; RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: RT Sordaria macrospora, a model organism for fungal morphogenesis."; RL PLoS Genet. 6:E1000891-E1000891(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|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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CCC08898.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CABT02000007; CCC08898.1; -; Genomic_DNA. DR RefSeq; XP_003344526.1; XM_003344478.1. DR STRING; 771870.F7VTR0; -. DR GeneID; 10801820; -. DR KEGG; smp:SMAC_07534; -. DR VEuPathDB; FungiDB:SMAC_07534; -. DR eggNOG; KOG1080; Eukaryota. DR HOGENOM; CLU_004391_0_0_1; -. DR InParanoid; F7VTR0; -. DR OMA; CHMTALF; -. DR OrthoDB; 950362at2759; -. DR Proteomes; UP000001881; 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:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR CDD; cd12302; RRM_scSet1p_like; 1. 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; IPR035979; RBD_domain_sf. 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; SSF54928; RNA-binding domain, RBD; 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 Reference proteome {ECO:0000313|Proteomes:UP000001881}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 1172..1289 FT /note="SET" FT /evidence="ECO:0000259|PROSITE:PS50280" FT DOMAIN 1298..1314 FT /note="Post-SET" FT /evidence="ECO:0000259|PROSITE:PS50868" FT REGION 1..182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 402..460 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 558..609 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 669..794 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 844..922 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 943..984 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..82 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 96..163 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..439 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 561..609 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 690..706 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 732..790 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 871..897 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 907..922 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 943..976 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1314 AA; 145987 MW; B8C33CC77E37A03F CRC64; MSRSSGASFA QFFPAAPRAA RDRATERERA RMRAQASPPT QPVDTNGHRT PLSSFTSNRS DDGASPGRSH ITSLNHSSSA GADATRPPLL EDSESLPGDT LNTVGSASSH ASTSSSIFSS STRQPAMASA SVRNSHTHNS NTPLTTADSP SSLYLSTSLH AKPHSVSPHH ADKQNGLTPT LNGSATEFLV PLPDGTDRVP LRNPSRSVLC TICTYDPLLD KKLSSSEKKR RNLYTRIMAW YNDEDDASPS DPRLAHGGKL SYINVNFHLP KAQLIDAPSN LKPYPYDPKT SCGPGPPVQI LVRGFNPLIA FTKVTTIFAS FGDIAESSNK MHPETGSYLG FATIRYKDSK PTPSRPVPVP AHQAARRAVR GMHGRRIEAS QVRVEFDPEG RKSKALMEAV LKKSRETSQP PSAAYKIPTG PKPRAGEVIP GPPPTAPKGP AAHRALGGSE AGWTSTKPRH PSIIENEPIL NHIKSEPYIF VAHDYVPVMP TTVAHMKKRL KQYGFDDIRA DRTGYYIIFR DSHYGRDEAG KCYNSANDTA FFTYSMVMEL HLFGTVGTSS KTSEDHRRHS YSSEKRPPPE HRQRDDQDRR RRDEEADIEE EKKQRAKNLD PVKEAAEVIR REMTEHLLKT IRTKITLPAV FDYLNPVNHA AKRRKLNIDD SHSGTIPSIV FDDSEGRSSP VGTPNSRADP IERRTARADV STLRVRKLKS RGVNARKHGF NDPFARARPT QRVDLRSLHH RLNSDSDDDS DDGVDNRYSM IRDTEEPESR PRSRMSSEED RNKEETGSWV AGEDDSMTEA SFALNDTSAL LRKRKLDLPV ETAIKRQKKA EELFEATIAP IETQLPSKEQ SVESATLPGT EAALDGLPDA DVKAEPTEDK ETDDSRLPTP QPDNTKLKKK GKAKKKSKKQ IFEEREALKK QQQEIYEREA LRAAGIEDIE ATPEAEAKSK AGEPEAVPEP ELEKGEAPEA PAIESKPDLD PELYPSEPVN ALVLPKDFHL DIGTLKLVPL QGEDGPDTQR LQRKFGTGKL ECDAELWLWK RNRIRQLNSE DGSKDKPVGI GGYYVPNPTG CARTEGVKKI LNSEKSKYLP HHIKVKKARE EREKNAKNGN INSVAAAAEA ARLAADSLVA KGNSRANRVN NRRYVAEIND QRKNFGQDSD VLRFNQLKKR KKPVKFARSA IHNWGLYAME NINKDDMIIE YVGEEVRQQI AELREARYLK SGIGSSYLFR IDDNTVIDAT KKGGIARFIN HSCMPNCTAK IIKVEGSKRI VIYALRDIAQ NEELTYDYKF EREIGSTDRI PCLCGTAACK GFLN //