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IF1C_ANEMR
ID   IF1C_ANEMR              Reviewed;          78 AA.
AC   B0YPR0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 46.
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   Aneura mirabilis (Parasitic liverwort) (Cryptothallus mirabilis).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Jungermanniopsida; Metzgeriidae; Metzgeriales; Aneuraceae; Aneura.
OX   NCBI_TaxID=280810;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18056074; DOI=10.1093/molbev/msm267;
RA   Wickett N.J., Zhang Y., Hansen S.K., Roper J.M., Kuehl J.V., Plock S.A.,
RA   Wolf P.G., dePamphilis C.W., Boore J.L., Goffinet B.;
RT   "Functional gene losses occur with minimal size reduction in the plastid
RT   genome of the parasitic liverwort Aneura mirabilis.";
RL   Mol. Biol. Evol. 25:393-401(2008).
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; EU043314; ABS54508.1; -; Genomic_DNA.
DR   RefSeq; YP_001687246.1; NC_010359.1.
DR   AlphaFoldDB; B0YPR0; -.
DR   SMR; B0YPR0; -.
DR   GeneID; 5952192; -.
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   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; 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..78
FT                   /note="Translation initiation factor IF-1, plastid"
FT                   /id="PRO_0000338955"
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   78 AA;  8955 MW;  A3B3CB21120F50B6 CRC64;
     MKKQDLIDME GVVTESLPNA MFRVCLDNGC QVLTHISGRI RRNYIRILPG DRVRVESSPY
     DLTKGRITYR LRAKSSTD
 
 
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