ID A0A0L1J2A2_ASPNO Unreviewed; 815 AA.
AC A0A0L1J2A2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative histone-lysine N-methyltransferase (Ash1) {ECO:0000313|EMBL:KNG85872.1};
GN ORFNames=ANOM_003651 {ECO:0000313|EMBL:KNG85872.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG85872.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG85872.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG85872.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KNG85872.1}.
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DR EMBL; JNOM01000138; KNG85872.1; -; Genomic_DNA.
DR RefSeq; XP_015406795.1; XM_015548908.1.
DR AlphaFoldDB; A0A0L1J2A2; -.
DR STRING; 1509407.A0A0L1J2A2; -.
DR GeneID; 26805455; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000037505; 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:KNG85872.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNG85872.1}.
FT DOMAIN 407..453
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 464..580
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 588..604
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 90737 MW; A578704BF5EBFC75 CRC64;
MESQLSSAGA PPATPATLSD LNKHAHEPAD DTMAFEYSEQ LLTPENSRSE TSSNNENAST
EEKPTARRRS TRVTRASLRG EAQLDGDMEI DNQGTLSTAG ENDSAVSEEA LLDKAEGGKR
SQASHLRHSI AVMESWSEAT LAQDNMETEG DHPMAPDTPV SKSSQELQAS DMGTSLQQRT
LRKRVERILT EEGGSHKGKI TETAKETKSP VRRSSRLSLL EKASDLVGRA SSILGKRSRD
VVGKGKELGR RASLRPRITA PKEEPVKAAS EAPAAKKRRV SESDLPAKIQ ENEDTEQEAP
KPVTRSKTKR WLAHGLYTGQ EYTESRPLQS RNRNAKRRSQ GPTQRRLLPM PMFAGDRLLK
QGRDFELPFD IFSPLPSGQP KPNEWRKTNK NVFVGEASSI WRANKPLELS KCMCAEETGC
DEECQNRYMF YECDDSNCGV GPECGNRNFE ELKQRTKVGG KYNIGVEVIK TEDRGYGVRS
NRTFEPNQVI VEYTGEIITQ AECEKRMRTI YKKNECYYLM YFDQNMIIDA TRGSIARFVN
HSCEPNCRME KWTVAGKPRM ALFAGDRGIM TGDELTYDYN FDPYSQKNVQ QCRCGSDRCR
GILGPRPREK EQRSKEKELR AENEKKSSSK NNNKKASITK QKVLSGSTSR VNKRQLLGPK
SIKSGVKKVV SKARSSASKA TTTSKTSSKT SVSTKATKTT SKKAIATPAR RQVKKDNARS
KKEVKLPKVK TTKTKARKPM QTTKTQSAPS TSKLSRPSEK TKAKILQAAK GTNTRKRTVK
KEDTKTKSPA KRTSKVKEST LRGKTASKAA KNPKA
//
