ID A0A0S3R2E9_PHAAN Unreviewed; 258 AA.
AC A0A0S3R2E9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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 Name=Vigan.01G255300 {ECO:0000313|EMBL:BAT74793.1};
GN ORFNames=VIGAN_01255300 {ECO:0000313|EMBL:BAT74793.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT74793.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT74793.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR EMBL; AP015034; BAT74793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R2E9; -.
DR Proteomes; UP000291084; Chromosome 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:SF140; 14-3-3-LIKE PROTEIN GF14 IOTA; 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:UP000291084}.
FT DOMAIN 7..248
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 237..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 60
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 133
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 258 AA; 29431 MW; 3178253FC36954FC CRC64;
MSSEKERETQ VYIAKLSEQA ERYEEMVECM KAIAKLDLEL TVEERNLLSV GYKNVIGARR
ASWRIMSSIE QKEESKGNES NAKMIKNYRQ KVEEELSKIC SDILSIIDKH LVPSSTSGEA
TVFYYKMKGD YYRYLAEFKT DQERKEAAEQ SLKGYEAALA AANTDLPSTH PIRLGLALNF
SVFYYEIMNS PERACHLAKQ AFDEAIAELD TLSEESYKDS TLIMQLLRDN LTLWTSDLPE
DGGDEIKPEE IKPAAPEH
//