ID A0A1B8B3Q6_FUSPO Unreviewed; 273 AA.
AC A0A1B8B3Q6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=14-3-3 domain-containing protein {ECO:0000259|SMART:SM00101};
GN ORFNames=FPOA_01279 {ECO:0000313|EMBL:OBS27336.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS27336.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS27336.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS27336.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141}.
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:OBS27336.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LYXU01000001; OBS27336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8B3Q6; -.
DR STRING; 36050.A0A1B8B3Q6; -.
DR OMA; EQHVTII; -.
DR Proteomes; UP000091967; Unassembled WGS sequence.
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:SF39; 14-3-3 PROTEIN (EUROFUNG); 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000091967}.
FT DOMAIN 5..246
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 236..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 131
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 273 AA; 30312 MW; 821E71A8946C5F18 CRC64;
MATERESKTF LARLCEQAER YDEMVTYMKE VAKLGGELTV DERNLLSVAY KNVVGTRRAS
WRIISSIEQK EESKGSDKHV STIKDYRNKI ETELEKVCQD VLDVLDDFLI PNAATGESKV
FYHKMKGDYH RYLAEFASGE KRKGAATAAH DAYKSATDVA QTELTPTHPI RLGLALNFSV
FYYEILNSPD RACHLAKQAF DDAIAELDSL SEESYRDSTL IMQLLRDNLT LWTSSDSAEG
EAAGAADAPK KEEGEAAKPA EEPAEETAPA PAS
//