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Database: UniProt
Entry: A0A2G5CT69_AQUCA
LinkDB: A0A2G5CT69_AQUCA
Original site: A0A2G5CT69_AQUCA 
ID   A0A2G5CT69_AQUCA        Unreviewed;       145 AA.
AC   A0A2G5CT69;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN   ORFNames=AQUCO_03700026v1 {ECO:0000313|EMBL:PIA34472.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA34472.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA34472.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025502,
CC       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   EMBL; KZ305054; PIA34472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5CT69; -.
DR   STRING; 218851.A0A2G5CT69; -.
DR   InParanoid; A0A2G5CT69; -.
DR   OrthoDB; 2919581at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
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:SF0; 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:UP000230069}.
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;  16426 MW;  9C40FB72D21C8950 CRC64;
     MPKNKGKGGK NRKRGKNEAD DEKRELVFKE DGQEYAQVLR MLGNGRCEAT CIDGVKRLCH
     IRGKMHKKVW IAAGDIILVG LRDYQDDKAD VILKYMPDEA RLLKAYGELP ENTRLNEGIA
     GGIDIDEDGP DDDYVEFEDE DIDKI
//
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