ID W6V2S5_ECHGR Unreviewed; 197 AA.
AC W6V2S5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN ORFNames=EGR_04837 {ECO:0000313|EMBL:EUB60279.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB60279.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB60279.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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}.
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:EUB60279.1}.
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DR EMBL; APAU02000032; EUB60279.1; -; Genomic_DNA.
DR AlphaFoldDB; W6V2S5; -.
DR STRING; 6210.W6V2S5; -.
DR EnsemblMetazoa; XM_024494086.1; XP_024351475.1; GeneID_36340552.
DR OMA; SHVHYKG; -.
DR OrthoDB; 2919581at2759; -.
DR Proteomes; UP000019149; 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:UP000019149}.
FT DOMAIN 22..96
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 197 AA; 22465 MW; 6CD5D35D9F417AF9 CRC64;
MPKNKGKGGK NRRRGKNENE GQKRALIYRE EGQQYAKVER LLGNGRLEAY CFDGVKRLCH
IRGKMRKKVW INSGDIILVS LRDYQDQKAD VILKYLNDEA RTLKSIGEIP DTVNLDENDD
IEFDANAAMP DDDLVVRNSN SDMPPSSSEE ESSEDEEDDD EEEDGDEGAP FGSHVHYKGE
FAGSTNRWDN KKSHKRK
//
