ID   A0A319ACF3_ASPLB        Unreviewed;       260 AA.
AC   A0A319ACF3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Putative 14-3-3 family protein ArtA {ECO:0000313|EMBL:PYH57726.1};
GN   ORFNames=BO96DRAFT_335011 {ECO:0000313|EMBL:PYH57726.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH57726.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH57726.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH57726.1,
RC   ECO:0000313|Proteomes:UP000247441};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC       {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR   EMBL; KZ821346; PYH57726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319ACF3; -.
DR   OrthoDB; 920089at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   CDD; cd11309; 14-3-3_fungi; 1.
DR   Gene3D; 1.20.190.20; 14-3-3 domain; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR036815; 14-3-3_dom_sf.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; 14-3-3 PROTEIN; 1.
DR   PANTHER; PTHR18860:SF17; 14-3-3 PROTEIN EPSILON; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3 protein; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          3..244
FT                   /note="14-3-3"
FT                   /evidence="ECO:0000259|SMART:SM00101"
FT   REGION          234..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            56
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT   SITE            129
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ   SEQUENCE   260 AA;  28972 MW;  6ED454A21A9B27E0 CRC64;
     MGHEDAVYLA KLAEQAERYE EMVENMKVVA SADVELTVEE RNLLSVAYKN VIGARRASWR
     IVTSIEQKEE SKGNESQVSL IKEYRQKIEA ELAKICDDIL EVLDKHLIPS AQSGESKVFY
     HKMKGDYHRY LAEFAVGDRR KGAADASLEA YKAATEVAQT DLAPTHPIRL GLALNFSVFY
     YEILNSPDQA CHLAKLAFDD AIAELDTLSE ESYKDSTLIM QLLRDNLTLW TSSEAEPAAE
     ASAPAEKKEE APAEGEKPAE
//