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Database: UniProt
Entry: W9CQX2_SCLBF
LinkDB: W9CQX2_SCLBF
Original site: W9CQX2_SCLBF 
ID   W9CQX2_SCLBF            Unreviewed;       265 AA.
AC   W9CQX2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=TH14-3-3 like protein {ECO:0000313|EMBL:ESZ98241.1};
GN   ORFNames=SBOR_1337 {ECO:0000313|EMBL:ESZ98241.1};
OS   Sclerotinia borealis (strain F-4128).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ98241.1, ECO:0000313|Proteomes:UP000019487};
RN   [1] {ECO:0000313|EMBL:ESZ98241.1, ECO:0000313|Proteomes:UP000019487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX   PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA   Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT   "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT   pathogenic fungus.";
RL   Genome Announc. 2:E0117513-E0117513(2014).
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:ESZ98241.1}.
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DR   EMBL; AYSA01000046; ESZ98241.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9CQX2; -.
DR   STRING; 1432307.W9CQX2; -.
DR   HOGENOM; CLU_058290_0_0_1; -.
DR   OrthoDB; 920089at2759; -.
DR   Proteomes; UP000019487; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019487}.
FT   DOMAIN          4..244
FT                   /note="14-3-3"
FT                   /evidence="ECO:0000259|SMART:SM00101"
FT   REGION          234..265
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   265 AA;  29626 MW;  E9015B93EC941D92 CRC64;
     MGYEDSVYLA KLAEQAERYE EMVENMKSVA SEDQELSVEE RNLLSVAYKN VIGARRASWR
     IVTSIEQKEE SKGNSSQVTL IKEYRQKIEA ELAKICEDIL EVLDKHLIPS AKSGESKVFY
     HKMKGDYHRY LAEFAIGDKR KESADKSLEA YKNATEVAQT DLAPTHPIRL GLALNFSVFY
     YEILNSPDQA CHLAKQAFDD AIAELDTLSE ESYKDSTLIM QLLRDNLTLW TSSEAEPTAS
     DAAAAPAETK EAEAAVPAEE KSAAE
//
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