ID   IF1C_ANGEV              Reviewed;          89 AA.
AC   A2T368;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 53.
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   Angiopteris evecta (Mule's foot fern) (Polypodium evectum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Marattiidae; Marattiales; Marattiaceae; Angiopteris.
OX   NCBI_TaxID=13825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Roper J.M., Hansen S.K., Wolf P.G., Karol K.G., Mandoli D.F.,
RA   Everett K.D.E., Kuehl J.V., Boore J.L.;
RT   "The complete plastid genome sequence of Angiopteris evecta (G. Forst.)
RT   Hoffm. (Marattiaceae).";
RL   Am. Fern J. 97:95-106(2007).
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; DQ821119; ABG79635.1; -; Genomic_DNA.
DR   RefSeq; YP_001023736.1; NC_008829.1.
DR   AlphaFoldDB; A2T368; -.
DR   SMR; A2T368; -.
DR   GeneID; 4788261; -.
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..89
FT                   /note="Translation initiation factor IF-1, chloroplastic"
FT                   /id="PRO_0000338956"
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   89 AA;  10413 MW;  37084E74E656E352 CRC64;
     MKKQDLIDME GIVTESLPNA MFRVCLDNGC QVLTHISGKI RRNYIRILPG DRVRVELSPY
     DLTKGRIIYR LRNKYPNGIS QEVFRSMRD