ID A0A2S4UZ69_9BASI Unreviewed; 144 AA.
AC A0A2S4UZ69;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN ORFNames=PSTT_11731 {ECO:0000313|EMBL:POW02495.1};
OS Puccinia striiformis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27350 {ECO:0000313|EMBL:POW02495.1, ECO:0000313|Proteomes:UP000239156};
RN [1] {ECO:0000313|EMBL:POW02495.1, ECO:0000313|Proteomes:UP000239156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-210 {ECO:0000313|EMBL:POW02495.1,
RC ECO:0000313|Proteomes:UP000239156};
RA Xia C.;
RT "Gene loss provides genomic basis for host adaptation in cereal stripe rust
RT fungi.";
RL Submitted (DEC-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 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:POW02495.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PKSL01000141; POW02495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4UZ69; -.
DR VEuPathDB; FungiDB:PSHT_14926; -.
DR VEuPathDB; FungiDB:PSTT_11731; -.
DR Proteomes; UP000239156; 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:UP000239156}.
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"
SQ SEQUENCE 144 AA; 16667 MW; 80123C575D221D34 CRC64;
MPKNKGKGGK NRRRGKNENE CEKRELVFKE DGQEYAQVTK MLGNGRLEAM CFDGEKRLAH
IRGKMRKKVW INQGDIILIS LRDFQDDKAD VIQKYTTDEA RNLKAYGELP ENAKINETDT
FGPGEDDECN FEFEEVIHIF IPIL
//
