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Database: UniProt
Entry: A0A179FZJ5_METCM
LinkDB: A0A179FZJ5_METCM
Original site: A0A179FZJ5_METCM 
ID   A0A179FZJ5_METCM        Unreviewed;       268 AA.
AC   A0A179FZJ5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=14-3-3 protein {ECO:0000313|EMBL:OAQ70551.1};
GN   ORFNames=VFPPC_03003 {ECO:0000313|EMBL:OAQ70551.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ70551.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ70551.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ70551.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC       {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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:OAQ70551.1}.
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DR   EMBL; LSBJ02000002; OAQ70551.1; -; Genomic_DNA.
DR   RefSeq; XP_018147088.1; XM_018282562.1.
DR   AlphaFoldDB; A0A179FZJ5; -.
DR   STRING; 1380566.A0A179FZJ5; -.
DR   GeneID; 28846556; -.
DR   KEGG; pchm:VFPPC_03003; -.
DR   OrthoDB; 920089at2759; -.
DR   Proteomes; UP000078397; Chromosome 2.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397}.
FT   DOMAIN          3..244
FT                   /note="14-3-3"
FT                   /evidence="ECO:0000259|SMART:SM00101"
FT   REGION          234..268
FT                   /note="Disordered"
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   268 AA;  29849 MW;  23EAC95A55FE4B0B CRC64;
     MGHEDAVYLA KLAEQAERYE EMVDNMKIVA SEDRDLTVEE RNLLSVAYKN VIGARRASWR
     IVTSIEQKEE SKGNSSQVTL IKEYRQKIEA ELAKICDDIL DVLDQHLIPS AKSGESKVFY
     HKMKGDYHRY LAEFAIGDRR KDSADKSLEA YKAATEVAQT ELPPTHPIRL GLALNFSVFY
     YEILNAPDQA CHLAKQAFDD AIAELDTLSE ESYKDSTLIM QLLRDNLTLW TSSEAETGAT
     GQADAPAKEE PAAAAEAPAA TEETKASE
//
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