ID   IF1C_STAPU              Reviewed;          77 AA.
AC   Q32RV0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 58.
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   Staurastrum punctulatum (Green alga) (Cosmoastrum punctulatum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC   Desmidiales; Desmidiaceae; Staurastrum.
OX   NCBI_TaxID=102822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequences of the charophycean green algae
RT   Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT   extensive changes during the evolution of the Zygnematales.";
RL   BMC Biol. 3:22-22(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX45696.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY958085; AAX45696.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_636426.1; NC_008116.1.
DR   AlphaFoldDB; Q32RV0; -.
DR   SMR; Q32RV0; -.
DR   GeneID; 4108652; -.
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..77
FT                   /note="Translation initiation factor IF-1, chloroplastic"
FT                   /id="PRO_0000226953"
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   77 AA;  8877 MW;  04B19485F0F5B35F CRC64;
     MRKQNLIEME GIVTESLPNA MFRVCLDNGC QVLAHISGKI RKNYIRILLG DRVKVELSPY
     DLTKGRITYR LRTRSPS