ID K9JAN0_9LILI Unreviewed; 77 AA. AC K9JAN0; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 24-JAN-2024, entry version 35. DE RecName: Full=Translation initiation factor IF-1, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00075}; GN Name=infA {ECO:0000256|HAMAP-Rule:MF_00075, GN ECO:0000313|EMBL:ADI88672.1}; OS Dioscorea exalata. OG Plastid; Chloroplast {ECO:0000313|EMBL:ADI88672.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae; OC Dioscorea. OX NCBI_TaxID=374973 {ECO:0000313|EMBL:ADI88672.1}; RN [1] {ECO:0000313|EMBL:ADI88672.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=68 {ECO:0000313|EMBL:ADI88672.1}; RA Hang Y.Y., Gao X., Guo J.L., Zhou Y.F., Peng B.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00003935, ECO:0000256|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:0000256|ARBA:ARBA00011599, CC ECO:0000256|HAMAP-Rule:MF_00075}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_00075}. CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000256|ARBA:ARBA00010939, CC ECO:0000256|HAMAP-Rule:MF_00075}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GQ265210; ADI88672.1; -; Genomic_DNA. DR AlphaFoldDB; K9JAN0; -. DR SMR; K9JAN0; -. 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; Nucleic acid-binding proteins; 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; IPR003029; S1_domain. DR InterPro; IPR004368; TIF_IF1. DR NCBIfam; TIGR00008; infA; 1. DR PANTHER; PTHR33370; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1. DR PANTHER; PTHR33370:SF1; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1. DR Pfam; PF01176; eIF-1a; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ADI88672.1}; KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP- KW Rule:MF_00075}; Plastid {ECO:0000313|EMBL:ADI88672.1}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00075}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}. FT DOMAIN 1..71 FT /note="S1-like" FT /evidence="ECO:0000259|PROSITE:PS50832" SQ SEQUENCE 77 AA; 9061 MW; 5D8C6ACA348DA8D6 CRC64; MKEQKLIHEG VIIESLPNGM FRVRLDNEDL ILGYVSGRIR RSFIRILPGD RVKIEVSRYD STKGRIIYRL RNKDSND //