ID A0A0N4TK63_BRUPA Unreviewed; 205 AA.
AC A0A0N4TK63;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN ORFNames=BPAG_LOCUS8678 {ECO:0000313|EMBL:VDN89864.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000871601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0000871601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN89864.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the 43S pre-initiation complex (43S PIC), which
CC binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated
CC region, and locates the initiation codon. This protein enhances
CC formation of the cap-proximal complex. Together with EIF1, facilitates
CC scanning, start codon recognition, promotion of the assembly of 48S
CC complex at the initiation codon (43S PIC becomes 48S PIC after the
CC start codon is reached), and dissociation of aberrant complexes. After
CC start codon location, together with EIF5B orients the initiator
CC methionine-tRNA in a conformation that allows 60S ribosomal subunit
CC joining to form the 80S initiation complex. Is released after 80S
CC initiation complex formation, just after GTP hydrolysis by EIF5B, and
CC before release of EIF5B. Its globular part is located in the A site of
CC the 40S ribosomal subunit. Its interaction with EIF5 during scanning
CC contribute to the maintenance of EIF1 within the open 43S PIC. In
CC contrast to yeast orthologs, does not bind EIF1.
CC {ECO:0000256|RuleBase:RU004365}.
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 -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|RuleBase:RU004364}.
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DR EMBL; UZAD01013138; VDN89864.1; -; Genomic_DNA.
DR STRING; 6280.A0A0N4TK63; -.
DR WBParaSite; BPAG_0000871601-mRNA-1; BPAG_0000871601-mRNA-1; BPAG_0000871601.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; 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:UP000278627}.
FT DOMAIN 22..96
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 23073 MW; 35E9C8025F82DFCB CRC64;
MPKNKGKGGK NRRRGKNEND IMKRELIYKE PGQEYAQVIK MLGNGRLNAN CFDGKPRLCH
IRGKLRKKVW INTGDIILIG LRDYQDDKAD VILKYNPDEA RNLKACGQLP ENAKLNEGGD
DLDEGGVEFG AFLPYLADTG ALSDEDNEGS GNEDLPSIGS DSDEDEDDEE EESEDSDDDR
ITEERLARSY VKPGARDRPQ KKNKW
//
