ID   IF1C_SACOF              Reviewed;         107 AA.
AC   Q6ENS9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Translation initiation factor IF-1, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000255|HAMAP-Rule:MF_00075};
OS   Saccharum officinarum (Sugarcane).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Saccharum;
OC   Saccharum officinarum complex.
OX   NCBI_TaxID=4547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15449542; DOI=10.1093/dnares/11.2.93;
RA   Asano T., Tsudzuki T., Takahashi S., Shimada H., Kadowaki K.;
RT   "Complete nucleotide sequence of the sugarcane (Saccharum officinarum)
RT   chloroplast genome: a comparative analysis of four monocot chloroplast
RT   genomes.";
RL   DNA Res. 11:93-99(2004).
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit
CC       to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps
CC       modulate mRNA selection, yielding the 30S pre-initiation complex (PIC).
CC       Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are
CC       released leaving the mature 70S translation initiation complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00075}.
CC   -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation
CC       complex which assembles on the 30S ribosome in the order IF-2 and IF-3,
CC       IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at
CC       any time during PIC assembly. {ECO:0000255|HAMAP-Rule:MF_00075}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_00075}.
CC   -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00075}.
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DR   EMBL; AP006714; BAD27327.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6ENS9; -.
DR   SMR; Q6ENS9; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04451; S1_IF1; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00075; IF_1; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR004368; TIF_IF1.
DR   PANTHER; PTHR33370; PTHR33370; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00008; infA; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Initiation factor; Plastid; Protein biosynthesis; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..107
FT                   /note="Translation initiation factor IF-1, chloroplastic"
FT                   /id="PRO_0000095950"
FT   DOMAIN          8..83
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
FT   REGION          81..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   107 AA;  12431 MW;  CE1DCD14F4F7BBAD CRC64;
     MTEKKNRREK KNPREAKVTF EGLVTEALPN GMFRVRLEND TIILGYISGK IRSSSIRILM
     GDRVKIEVSR YDSSKGRIIY RLPHKDSKRT EDSKDTEDLK DTKDSKD