ID A0A0L9TX80_PHAAN Unreviewed; 844 AA.
AC A0A0L9TX80;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=14-3-3 domain-containing protein {ECO:0000259|SMART:SM00101};
GN ORFNames=LR48_Vigan02g093900 {ECO:0000313|EMBL:KOM34789.1};
OS Phaseolus angularis (Azuki bean) (Vigna 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=3914 {ECO:0000313|EMBL:KOM34789.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141}.
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DR EMBL; CM003372; KOM34789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9TX80; -.
DR STRING; 3914.A0A0L9TX80; -.
DR EnsemblPlants; KOM34789; KOM34789; LR48_Vigan02g093900.
DR Gramene; KOM34789; KOM34789; LR48_Vigan02g093900.
DR Proteomes; UP000053144; Chromosome 2.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08774; 14-3-3; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 1.20.190.20; 14-3-3 domain; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR18860; 14-3-3 PROTEIN; 1.
DR PANTHER; PTHR18860:SF86; GENERAL REGULATORY FACTOR 2; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; 14-3-3 protein; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT DOMAIN 1..154
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 443..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 672..755
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94346 MW; BDFA5CA5BC24C665 CRC64;
MVDAMKKVAK LDDELSVEER NLFSVGYKNV VGSRRDSWMI LSSIEMKGDY YWYLAEFKAG
NEKNEVADQS LKAYQTIATT VESELQPTHP IRLGLPLNFS MFYYEIMNSP ETACHLAKQV
FGVVGLRLGY GVLNKVALEF PSVFWDDTVE HFGATPEERN SRGHCFMFWN VRKTVGDPVL
IALVVCRNPF SYGAYSYVAV GASGEDYDIL GILVNNCLFF AGEATCQKQP DTIGGAMMSG
LREPSRSKLC CLALPSRREP VKDLPMPKHG SSFCGPFIFG RGFVLVSAPC DYRFQDVEIL
PRSNFRKWVW VGKHVLCPCW WELRRLRIRT TDCGNFFTGG IPIDDASLEL VGDVTVIPGY
DWATHDASLF ASEYGTKKAL VWRIGWLYIV KDMEDSRLIR ASPCESSTLS PCRLSARGLV
ECLRHEDCER MAFDIMSAPP PRKSNFMASR KGVGASSSSG SERVAPTALR PPTNKRASSS
SRIPVVPPID SKACLAVTTV VPPGVVAAAG NDPPQNPPVV FLDPSSEVAT TFVQPLVRKR
KGHREGERPA SKKGRKEKEG SSSRFSSKKG RKGKEGSSSR PLLDGVFIPA FNISERTNFH
MSSTHRALIE PLWESELTTA MLEMSTRAAS LAWYLWKYAD WRGAEHVRAE LLAEKKISDD
LRAAMEEVLL AQVEYDKKND ELQVELDEAK EKLAKTTDRL RDARANYDRL VGECGQLKVV
VARQKKMESG LLQKNQALAD DLAKAKEKIS ELETGIVFEH EEGGTFHSPS DQVDSGSIWN
SLFINLVFRT IRAAVVLWEE HGVHCPNRLT VVPFGTRRSS TWIFARSEQQ WFYGKNSSFI
ARPS
//