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Database: UniProt
Entry: A0A1F8AG51_9EURO
LinkDB: A0A1F8AG51_9EURO
Original site: A0A1F8AG51_9EURO 
ID   A0A1F8AG51_9EURO        Unreviewed;       564 AA.
AC   A0A1F8AG51;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Myb-like DNA-binding domain protein {ECO:0000313|EMBL:OGM50671.1};
GN   ORFNames=ABOM_000436 {ECO:0000313|EMBL:OGM50671.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM50671.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM50671.1, 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:OGM50671.1}.
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DR   EMBL; LYCR01000002; OGM50671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8AG51; -.
DR   OrthoDB; 2788167at2759; -.
DR   Proteomes; UP000179179; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR018465; Scm3/HJURP.
DR   PANTHER; PTHR15992; HOLLIDAY JUNCTION RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR15992:SF5; HOLLIDAY JUNCTION RECOGNITION PROTEIN; 1.
DR   Pfam; PF10384; Scm3; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000313|EMBL:OGM50671.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  63116 MW;  FB1923E6D5051328 CRC64;
     MTERPLKRPR LSFATGTDDE PGDIDLQEAR AQNDQRLKSI FEGIFEKYGK DFTDVGDEID
     LQTGKIVVDN GHIQGMEDED DTGEEAPWLF DTENSALDDA ATAHNISQYS ETEAGGDLLE
     EDNTYLQHPQ AATQLQAGPN LSGPWESRES EALSAESDVD EDRSSVDSLL DTALSVQNGP
     DDPVRRKNLM DTDEVVTKKA KPTAETSTQS QILQKHSSIE AVDSVWRVPR ISGKFSTPPL
     SRSRPPVSFN AVRSASPPGA GSIWALPGKS RRTTDITKRR SARKHESSQH KWKPQSSPIM
     CDWSFAETPD GNESDDPLQE NYQPSPTPKG GLKIRGKRLG PDTPSRRKDL VDDCKVSPLR
     DDPASRLHQT SLNSAEDQRD TTEAANQPET TANNVALDTQ LVTKSDTKIH DISMEVTQDP
     KITPIGYQPK PQDSTSPSKR TRTTITPDEA RLIVVLKQVQ GKKWKEILDR LPWKKLAQLV
     QWNHLHWNER RANPPPLSKP WSSTERETLH DLKDQRGLTW HAIRTRLPGR SLAEIEFELL
     ILWVGDDVWN TEQQDGIAPS FSME
//
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