ID   IF1C_EPIVI              Reviewed;          77 AA.
AC   P30070;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Translation initiation factor IF-1, plastid {ECO:0000255|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000255|HAMAP-Rule:MF_00075};
OS   Epifagus virginiana (Beechdrops) (Orobanche virginiana).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Orobancheae; Epifagus.
OX   NCBI_TaxID=4177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1332054; DOI=10.1073/pnas.89.22.10648;
RA   Wolfe K.H., Morden C.W., Palmer J.D.;
RT   "Function and evolution of a minimal plastid genome from a
RT   nonphotosynthetic parasitic plant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10648-10652(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1404416; DOI=10.1007/bf00161168;
RA   Wolfe K.H., Morden C.W., Ems S.C., Palmer J.D.;
RT   "Rapid evolution of the plastid translational apparatus in a
RT   nonphotosynthetic plant: loss or accelerated sequence evolution of tRNA and
RT   ribosomal protein genes.";
RL   J. Mol. Evol. 35:304-317(1992).
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 {ECO:0000255|HAMAP-Rule:MF_00075}.
CC   -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00075}.
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DR   EMBL; M81884; AAA65861.1; -; Genomic_DNA.
DR   PIR; S78392; S78392.
DR   RefSeq; NP_054387.1; NC_001568.1.
DR   AlphaFoldDB; P30070; -.
DR   SMR; P30070; -.
DR   GeneID; 801422; -.
DR   GO; GO:0009536; C:plastid; 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   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; IPR004368; TIF_IF1.
DR   PANTHER; PTHR33370; PTHR33370; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00008; infA; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Plastid; Protein biosynthesis; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..77
FT                   /note="Translation initiation factor IF-1, plastid"
FT                   /id="PRO_0000095928"
FT   DOMAIN          1..71
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   77 AA;  9245 MW;  83C79081E1771DBD CRC64;
     MKEQKWIHEG LITESLTNGM FWVRLDNKDL IIGYVSGNIR HSFIRILPGD KVKIEVSRYN
     STRGRIIYRL RNKYYKD