ID A0A1F7ZI73_9EURO Unreviewed; 703 AA.
AC A0A1F7ZI73;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:OGM39151.1};
GN ORFNames=ABOM_012234 {ECO:0000313|EMBL:OGM39151.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM39151.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM39151.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM39151.1}.
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DR EMBL; LYCR01000275; OGM39151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZI73; -.
DR STRING; 109264.A0A1F7ZI73; -.
DR OrthoDB; 2695278at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR024688; Mac_dom.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR23416; SIALIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR23416:SF76; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF12464; Mac; 1.
DR Pfam; PF16628; Mac_assoc; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SMART; SM01266; Mac; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:OGM39151.1}.
FT DOMAIN 278..306
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 76981 MW; B9B2C369DC9B175E CRC64;
MTAVTSASMI NDHESEGSRT DHSPSRFTAV NGKDSVISAT PMSVPAVPGS ATDEDSRESS
EHCGRSGHDD TIHRHEERMR EGGNTKNDQE DRRSQRSSSH CAVSVTSKGK RKRSGSGAHV
DDAHFTHRAP KSPASHLDET TNQNAHPCTS NGSTTSQADQ DFKNTPPLVH ARLEGSEDSR
TSANTTWHEY DAQLVSQAQR AQQIDASDAQ LAEALQREAQ GHDVTQKNWS AVSRSLEGTT
QNEQSSSALV GFAQERPQPA VQVAPKRKRV FSNRTKTGCM TCRRRKKKCD EQHPACNNCI
RGGFLCEGYS SRSTWQKPSS GKTPVPLQSK EGYTDVGSQY VHDISQQHDR QQGLTEQLEA
GKMRSIIVDD SDRTTTQFNN SSPTGVGSGR GSWSKRSWPN TGHNAYITDH IAKSDYRDVP
SIHELPRESH PKTDYQIVPP IRELSHGTAH GKPGVSLFQG GIDQRPALAT NVDTSSPQAQ
ARMALSIEHQ LSARTVPGEE TEKDKMIRGE LYRPFDIHLV EERERCKAAL WRFNNACNPV
SGLSNKEQNR LLKEILVPPA SAVGSPPGVT SPRPTGSIGQ GAVVEAPFQC HYGYNVHIGE
DVMISESCLF VDDCPITIGA HTWIGPRVTI LSSMAHANMQ ERKGSQSRYQ GRPVTIEEDC
YVGAGCTIYP GVRLRRGAYV APGEVVKSDI VAYGFQGLKP SYM
//
