ID A0A409VGB8_9AGAR Unreviewed; 139 AA.
AC A0A409VGB8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN ORFNames=CVT26_000236 {ECO:0000313|EMBL:PPQ65276.1};
OS Gymnopilus dilepis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX NCBI_TaxID=231916 {ECO:0000313|EMBL:PPQ65276.1, ECO:0000313|Proteomes:UP000284706};
RN [1] {ECO:0000313|EMBL:PPQ65276.1, ECO:0000313|Proteomes:UP000284706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRW20 {ECO:0000313|EMBL:PPQ65276.1,
RC ECO:0000313|Proteomes:UP000284706};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
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:PPQ65276.1}.
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DR EMBL; NHYE01005656; PPQ65276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409VGB8; -.
DR STRING; 231916.A0A409VGB8; -.
DR InParanoid; A0A409VGB8; -.
DR OrthoDB; 2919581at2759; -.
DR Proteomes; UP000284706; 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:UP000284706}.
FT DOMAIN 18..92
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 139 AA; 15959 MW; 826DD1B8AB5F79EF CRC64;
MPKGGKNRRR GKNENEDDKR ELVFREDGQE YAQVIKMLGN GRLEAQCFDG EKRLAHIRGK
MRKKVWINQG DIVLLSLRDF QDDKADVIVK YTADEARNLK AYGELPENAK INETDTFGEE
DGECTFEFGD EGEVDIDDI
//
