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
//