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Database: UniProt
Entry: A0A1J0WDN8_9RHOB
LinkDB: A0A1J0WDN8_9RHOB
Original site: A0A1J0WDN8_9RHOB 
ID   A0A1J0WDN8_9RHOB        Unreviewed;        72 AA.
AC   A0A1J0WDN8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000256|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000256|HAMAP-Rule:MF_00075};
GN   ORFNames=BOO69_02590 {ECO:0000313|EMBL:APE42426.1};
OS   Sulfitobacter alexandrii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE42426.1, ECO:0000313|Proteomes:UP000181897};
RN   [1] {ECO:0000313|EMBL:APE42426.1, ECO:0000313|Proteomes:UP000181897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM1-D1 {ECO:0000313|EMBL:APE42426.1,
RC   ECO:0000313|Proteomes:UP000181897};
RA   Yang Q., Zhang X., Tian X.;
RT   "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT   associated with marine dinoflagellate Alexandrium minutum in East China
RT   Sea.";
RL   Submitted (NOV-2016) 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|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|HAMAP-Rule:MF_00075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075}.
CC   -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000256|ARBA:ARBA00010939,
CC       ECO:0000256|HAMAP-Rule:MF_00075}.
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DR   EMBL; CP018076; APE42426.1; -; Genomic_DNA.
DR   RefSeq; WP_005978431.1; NZ_CP018076.1.
DR   AlphaFoldDB; A0A1J0WDN8; -.
DR   SMR; A0A1J0WDN8; -.
DR   STRING; 1917485.BOO69_02590; -.
DR   GeneID; 78398490; -.
DR   KEGG; suam:BOO69_02590; -.
DR   OrthoDB; 9803250at2; -.
DR   Proteomes; UP000181897; 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; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00075};
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..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
SQ   SEQUENCE   72 AA;  8286 MW;  C2C7737C4BEA7FBF CRC64;
     MAKEDTLEFP GVVKELLPNA TFRVELENGH EIIAHTAGKM RKNRIRVLAG DKVQVEMTPY
     DLTKGRINYR FK
//
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