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Database: UniProt
Entry: A0A1S3VAW3_VIGRR
LinkDB: A0A1S3VAW3_VIGRR
Original site: A0A1S3VAW3_VIGRR 
ID   A0A1S3VAW3_VIGRR        Unreviewed;       145 AA.
AC   A0A1S3VAW3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN   Name=LOC106773194 {ECO:0000313|RefSeq:XP_014515395.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014515395.1};
RN   [1] {ECO:0000313|RefSeq:XP_014515395.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014515395.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Seems to be required for maximal rate of protein
CC       biosynthesis. Enhances ribosome dissociation into subunits and
CC       stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC       subunits. {ECO:0000256|RuleBase:RU004365}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family.
CC       {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|RuleBase:RU004364}.
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DR   RefSeq; XP_014515395.1; XM_014659909.2.
DR   AlphaFoldDB; A0A1S3VAW3; -.
DR   STRING; 3916.A0A1S3VAW3; -.
DR   EnsemblPlants; Vradi09g03720.1; Vradi09g03720.1; Vradi09g03720.
DR   GeneID; 106773194; -.
DR   Gramene; Vradi09g03720.1; Vradi09g03720.1; Vradi09g03720.
DR   KEGG; vra:106773194; -.
DR   OrthoDB; 2919581at2759; -.
DR   Proteomes; UP000087766; Chromosome 9.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd05793; S1_IF1A; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00216; aIF_1A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR001253; TIF_eIF-1A.
DR   InterPro; IPR018104; TIF_eIF-1A_CS.
DR   NCBIfam; TIGR00523; eIF-1A; 1.
DR   PANTHER; PTHR21668; EIF-1A; 1.
DR   PANTHER; PTHR21668:SF20; EUKARYOTIC TRANSLATION INITIATION FACTOR 4C; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS01262; IF1A; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181,
KW   ECO:0000256|RuleBase:RU004365};
KW   Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181,
KW   ECO:0000256|RuleBase:RU004365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          22..96
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   145 AA;  16361 MW;  92004B8EBE167C26 CRC64;
     MPKNKGKGGK NRKRGKNEAD DEKRELVFKE DGQEYAQVLR MLGNGRCEAM CIDGTKRLCH
     IRGKMHKKVW IAAGDIILVG LRDYQDDKAD VILKYMPDEA RLLKAYGELP DSTRLNEGIG
     AGLDEEDDGA GNDYIEFEDE DIDKI
//
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