ID A0A3M2T091_9EURO Unreviewed; 267 AA.
AC A0A3M2T091;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE SubName: Full=14-3-3 protein {ECO:0000313|EMBL:RMJ23229.1};
DE Flags: Fragment;
GN ORFNames=PHISP_05888 {ECO:0000313|EMBL:RMJ23229.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ23229.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ23229.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ23229.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-2017) 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:RMJ23229.1}.
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DR EMBL; RAQS01000261; RMJ23229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2T091; -.
DR STRING; 1960876.A0A3M2T091; -.
DR Proteomes; UP000272442; 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:UP000272442}.
FT DOMAIN 1..240
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 226..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 51
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 124
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RMJ23229.1"
SQ SEQUENCE 267 AA; 30228 MW; A5C20F1F8B7B35C2 CRC64;
KTFLARLCEQ AERYDEMVTF MKEVANIGGE LTVDERNLLS VAYKNVVGTR RASWRIISSI
EQKEESKGSE QHVSIIHDYR QKIENELERV CQDVLDVLDQ SLIPKAETGE SKVFYYKMKG
DYHRYLAEFA SGNKRKVAAT AAHEAYKNAT DVAQTELTPT HPIRLGLALN FSVFYYEILN
SPDRACHLAK QAFDDAIAEL DNLSEESYRD STLIMQLLRD NLTLWTSSDG NENEATSAPK
DEKPEEESAP VPEEKGEEAK PDPTPES
//
