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