ID A0A2G5TZ15_9PELO Unreviewed; 219 AA.
AC A0A2G5TZ15;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN Name=Cnig_chr_IV.g12808 {ECO:0000313|EMBL:PIC32498.1};
GN ORFNames=B9Z55_012808 {ECO:0000313|EMBL:PIC32498.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC32498.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392}.
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:PIC32498.1}.
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DR EMBL; PDUG01000004; PIC32498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TZ15; -.
DR STRING; 1611254.A0A2G5TZ15; -.
DR Proteomes; UP000230233; Chromosome iv.
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 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 Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233}.
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 133..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 219 AA; 25180 MW; 8E649437CFA916C6 CRC64;
MPKNKGKGGK NRRRGKNENF SMKRELELKE DGQEYGHVSK LLGNSRVHVY CFDGAQRVCH
IRGKLRKKAW INVGDILLIG LRDYQDDKGD VILKYHPGEA RRLKNDGWIP ENAKLNENDE
QDEEDVEFLE NVEEDGQPGD EAASNELSSD SDSDESEDEE VLDKEEESEE EESEEEEESD
EDLDDSDRIL KENMAAERIL KEDTRRGRNR GAKNKNGKK
//
