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IF1_DINSH
ID   IF1_DINSH               Reviewed;          72 AA.
AC   A8LS17;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=Dshi_0982;
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
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: Cytoplasm {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; CP000830; ABV92724.1; -; Genomic_DNA.
DR   RefSeq; WP_007205486.1; NC_009952.1.
DR   AlphaFoldDB; A8LS17; -.
DR   SMR; A8LS17; -.
DR   STRING; 398580.Dshi_0982; -.
DR   EnsemblBacteria; ABV92724; ABV92724; Dshi_0982.
DR   KEGG; dsh:Dshi_0982; -.
DR   eggNOG; COG0361; Bacteria.
DR   HOGENOM; CLU_151267_1_0_5; -.
DR   OMA; ECLRSAM; -.
DR   OrthoDB; 2066663at2; -.
DR   Proteomes; UP000006833; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..72
FT                   /note="Translation initiation factor IF-1"
FT                   /id="PRO_0000338818"
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   72 AA;  8312 MW;  37C765EB7A4CE88E CRC64;
     MAKEELLEFP GVVKELLPNA TFRVELENGH EIIAHTAGKM RKNRIRVLAG DKVQVEMTPY
     DLTKGRINYR FK
 
 
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