ID B8NV14_ASPFN Unreviewed; 789 AA. AC B8NV14; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 88. DE SubName: Full=Histone-lysine N-methyltransferase (Ash1), putative {ECO:0000313|EMBL:EED46643.1}; GN ORFNames=AFLA_103080 {ECO:0000313|EMBL:EED46643.1}; OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 OS / JCM 12722 / SRRC 167). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED46643.1, ECO:0000313|Proteomes:UP000001875}; RN [1] {ECO:0000313|EMBL:EED46643.1, ECO:0000313|Proteomes:UP000001875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}; RX PubMed=25883274; DOI=10.1128/genomeA.00168-15; RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E., RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.; RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes RT aflatoxin contamination of food and feed."; RL Genome Announc. 3:E0016815-E0016815(2015). 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; EQ963484; EED46643.1; -; Genomic_DNA. DR RefSeq; XP_002384179.1; XM_002384138.1. DR AlphaFoldDB; B8NV14; -. DR SMR; B8NV14; -. DR STRING; 332952.B8NV14; -. DR EnsemblFungi; EED46643; EED46643; AFLA_103080. DR VEuPathDB; FungiDB:AFLA_010555; -. DR eggNOG; KOG1083; Eukaryota. DR HOGENOM; CLU_004379_3_0_1; -. DR OMA; NCQNRYM; -. DR Proteomes; UP000001875; Unassembled WGS sequence. 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; 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 ECO:0000313|EMBL:EED46643.1}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EED46643.1}. FT DOMAIN 375..421 FT /note="AWS" FT /evidence="ECO:0000259|PROSITE:PS51215" FT DOMAIN 432..548 FT /note="SET" FT /evidence="ECO:0000259|PROSITE:PS50280" FT DOMAIN 556..572 FT /note="Post-SET" FT /evidence="ECO:0000259|PROSITE:PS50868" FT REGION 1..94 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 106..186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 205..270 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 284..315 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 571..627 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 642..789 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 8..28 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 58..73 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 126..147 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 148..169 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 207..270 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 571..599 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 600..627 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 643..675 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 677..698 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 713..730 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 749..778 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 789 AA; 87972 MW; 028AC025B96F3448 CRC64; MAFEYSEQLL TPENSRSETS SNNENASTEE KPPVRRRSTR VTRASLRGEA QLDGDMEIDN QGTLSTAGEN NPVVSGETLV DKAEGGKRSQ ASHLRHSIAV MESWSEATLA QGNMETEGDH PLAPDTPVSK SSQELQASDM GTSLQQRTLR KRVERILTEE GHGNKGKVTV TAKEIKSPVR RSSRLSLLEK ASDLVGRASS VLGKRSRDVM GKGKELGRRA SLRPRTTAPK EEPTKAASEA PAAKKRRVSE SDLPVKIQEN EEAVQEAPKP VVRSRTKRWL AHGLYTGQEH TESRPLQSRS RNAKRKSQGP TQRRLLPMPM FAGDRLLKQG RDFQLPFDIF SPLPSGQPKP NEWRKTNKNV FVGEASSIWR ANKPLELSKC MCAEETGCDE ECQNRYMFYE CDDTNCGVGP ECGNRNFEEL KQRTKAGGKY NIGVEVIKTE DRGYGVRSNR TFEPNQVIVE YTGEIITQAE CEKRMRTIYK NNECYYLMYF DQNMIIDATR GSIARFVNHS CEPNCRMEKW TVAGKPRMAL FAGDRGIMTG DELTYDYNFD PYSQKNVQQC RCGSDRCRGI LGPRPREKEQ RSKEKELRAE NEKKSSSKNN NEKASITKQK VLNGSTSRVN KRQLLGSKSI KSGVKKVVSK ARASASKATT ASRTSLKTTV STKTSKTTNK KATATPTRRQ VKKDNTKSKK EVKLPKVKTT KTKARAPASA RKPAQKNKTQ STPLTSKLSR PSEKTKAKIL QAAKGTNARR RTVKKEDTKP KSPTKRTSKA KETSPRGKAA SKAAKNTKA //