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Database: UniProt
Entry: A0A498HDI9_MALDO
LinkDB: A0A498HDI9_MALDO
Original site: A0A498HDI9_MALDO 
ID   A0A498HDI9_MALDO        Unreviewed;       146 AA.
AC   A0A498HDI9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN   ORFNames=DVH24_028089 {ECO:0000313|EMBL:RXH67942.1}, DVH24_028091
GN   {ECO:0000313|EMBL:RXH67944.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH67942.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH67942.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH67942.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) 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}.
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:RXH67942.1}.
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DR   EMBL; RDQH01000343; RXH67942.1; -; Genomic_DNA.
DR   EMBL; RDQH01000343; RXH67944.1; -; Genomic_DNA.
DR   RefSeq; XP_008342155.1; XM_008343933.2.
DR   RefSeq; XP_008342156.1; XM_008343934.2.
DR   RefSeq; XP_008353593.1; XM_008355371.2.
DR   RefSeq; XP_017179697.1; XM_017324208.1.
DR   AlphaFoldDB; A0A498HDI9; -.
DR   STRING; 3750.A0A498HDI9; -.
DR   EnsemblPlants; mRNA:MD17G0095800; mRNA:MD17G0095800; MD17G0095800.
DR   GeneID; 103404973; -.
DR   GeneID; 103417179; -.
DR   Gramene; mRNA:MD17G0095800; mRNA:MD17G0095800; MD17G0095800.
DR   KEGG; mdm:103404973; -.
DR   KEGG; mdm:103417179; -.
DR   OrthoDB; 2919581at2759; -.
DR   Proteomes; UP000290289; Chromosome 17.
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:UP000290289}.
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   146 AA;  16547 MW;  5146544626FDD2C3 CRC64;
     MPKNKGKGGK NRKRGKNEAD DEKRELVFKE DGQEYAQVLR MLGNGRCEAM CIDGTKRLCH
     IRGKMHKKVW IAAGDIILVG LRDYQDDKAD VILKYMPDEA RLLKAYGELP ENTRLNEGIA
     GGIDDEETEG GVDDYIEFED EDIDKI
//
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