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Database: UniProt
Entry: E6ZNQ5_SPORE
LinkDB: E6ZNQ5_SPORE
Original site: E6ZNQ5_SPORE 
ID   E6ZNQ5_SPORE            Unreviewed;       152 AA.
AC   E6ZNQ5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN   ORFNames=sr15129 {ECO:0000313|EMBL:CBQ68906.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ68906.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ68906.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
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}.
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DR   EMBL; FQ311433; CBQ68906.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZNQ5; -.
DR   EnsemblFungi; CBQ68906; CBQ68906; sr15129.
DR   VEuPathDB; FungiDB:sr15129; -.
DR   eggNOG; KOG3403; Eukaryota.
DR   HOGENOM; CLU_109098_0_1_1; -.
DR   OrthoDB; 2919581at2759; -.
DR   Proteomes; UP000008867; Chromosome 12.
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}.
FT   DOMAIN          21..96
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   REGION          104..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..152
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   152 AA;  17098 MW;  DF2286261975ADC2 CRC64;
     MPKNKGKGGK NRRRGKNDIG DKRELVLKDE GQAEYAQVLK MLGNGRLEAQ CFDGEKRLAH
     IRGKLRKKVW INQGDIILIS LRDFQDGKAD VIQKYNADEA RALKQQGELP ESAKINETDT
     FGEDDGGEIE FQEGSDDDDD DDSDDDDDLD DL
//
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