ID G2R2C4_THETT Unreviewed; 950 AA. AC G2R2C4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM}; GN ORFNames=THITE_2111453 {ECO:0000313|EMBL:AEO64992.1}; OS Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia OS terrestris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides; OC Thermothielavioides terrestris. OX NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO64992.1, ECO:0000313|Proteomes:UP000008181}; RN [1] {ECO:0000313|EMBL:AEO64992.1, ECO:0000313|Proteomes:UP000008181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181}; RX PubMed=21964414; DOI=10.1038/nbt.1976; RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I., RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M., RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P., RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P., RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J., RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S., RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W., RA Tsang A.; RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi RT Myceliophthora thermophila and Thielavia terrestris."; RL Nat. Biotechnol. 29:922-927(2011). CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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; CP003010; AEO64992.1; -; Genomic_DNA. DR RefSeq; XP_003651328.1; XM_003651280.1. DR AlphaFoldDB; G2R2C4; -. DR STRING; 578455.G2R2C4; -. DR GeneID; 11518285; -. DR KEGG; ttt:THITE_2111453; -. DR eggNOG; KOG1083; Eukaryota. DR HOGENOM; CLU_004379_1_0_1; -. DR OrthoDB; 950362at2759; -. DR Proteomes; UP000008181; Chromosome 2. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR Gene3D; 2.170.270.10; SET domain; 1. DR InterPro; IPR006560; AWS_dom. DR InterPro; IPR003616; Post-SET_dom. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR PANTHER; PTHR22884:SF512; N-METHYLTRANSFERASE (ASH1), PUTATIVE (AFU_ORTHOLOGUE AFUA_3G06480)-RELATED; 1. DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1. DR Pfam; PF17907; AWS; 1. DR Pfam; PF00856; SET; 1. DR SMART; SM00570; AWS; 1. DR SMART; SM00508; PostSET; 1. DR SMART; SM00317; SET; 1. DR SUPFAM; SSF82199; SET domain; 1. DR PROSITE; PS51215; AWS; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS50280; SET; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW Reference proteome {ECO:0000313|Proteomes:UP000008181}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 448..495 FT /note="AWS" FT /evidence="ECO:0000259|PROSITE:PS51215" FT DOMAIN 506..622 FT /note="SET" FT /evidence="ECO:0000259|PROSITE:PS50280" FT DOMAIN 630..646 FT /note="Post-SET" FT /evidence="ECO:0000259|PROSITE:PS50868" FT REGION 21..234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 291..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..701 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 738..760 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 778..836 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 849..950 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..53 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 135..159 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..212 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 307..321 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 653..673 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 787..822 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 849..893 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 950 AA; 101154 MW; C4CDD57AD994A205 CRC64; MATLEAAPTM AELDTLLLDA SSFSSSTPSD RSSANSASLS STPPTTISPD SMSLASEPDA AKPLSAAASS IEAVIASPKA PETAQQNEPR QQTPVGHDAI VVAEQPLPAE PPSNSRPRRA RSSLPVYNLA RLAGTDVHGR RRSKGDAGLE KRRRTVSEAT LAAPHDGATS DSTDAPAGTA QSPARIAPGA LPASPTTTRT ATRLSTPRSA RISKKSRSIR ASPHLTRRST RLSGAPVEDL ATKLSALNKR GKKAAQKALG GLSRELKRLQ DTNEFLHIDT RPVRYTVWSN GKYVDTDPSQ PTAPEPPRKK VKVDKNAAGE QETSETGKPE AGVPATNKPR VKKWLEKGLY AGQEAPVDIF QGLTAQEKKK LASIPELLRS SKPNRTFPLP MYNGLRILIH GRDFKLPFDI CNPLPPGQPK PAAYRTMTKN RFVGNAAAYW KKTPHFGDFA SKCVCKPEDG CGEDCQNRIM LYECDETNCN IGREYCTNRA FQDLQERTKK GGRYRVGVEV FKTPDRGYGV RSNRCFEPNQ IIMEYTGEII TEEECERRMN EEYKDNECYY LMSFDQNMII DATTGSIARF VNHSCSPNCR MIKWIVSGQP RMALFAGDRP IMTGEELTYD YNFDPFSAKN VQKCLCGSAN CRGVLGPKPK EVKPPKQPPK QPSEQEKKLG KGSSKVSAKG TGKGSAKAPG QSSAKPSAKR KLKDAFEFDG DDEVAAGTAK KRKLAATVGP KRTLSSASLK GVKGAAKGAA KKATKGATKG AVTAIKRGGL SISVAAKKRG LSSKSAKTKT VKKGATTTAL GRISKKTTYG KKSQTVATAT TTKAPKPKAA APSRSPSLTI VAAGVESAAS ASATATPVPQ TTPRKAAAAI PASSSSRKQL PKLTISGGKT SARKWTPSRK AIEAGLADKS PAAAASAKSS GASDGAQKTG KGLDLSRTPK IKLVNATKSN //