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}.
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; 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
//