GenomeNet

Database: UniProt
Entry: G2Z459_FLABF
LinkDB: G2Z459_FLABF
Original site: G2Z459_FLABF 
ID   G2Z459_FLABF            Unreviewed;        71 AA.
AC   G2Z459;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000256|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000256|HAMAP-Rule:MF_00075,
GN   ECO:0000313|EMBL:CCB70548.1};
GN   OrderedLocusNames=FBFL15_2550 {ECO:0000313|EMBL:CCB70548.1};
OS   Flavobacterium branchiophilum (strain FL-15).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB70548.1, ECO:0000313|Proteomes:UP000009186};
RN   [1] {ECO:0000313|EMBL:CCB70548.1, ECO:0000313|Proteomes:UP000009186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FL-15 {ECO:0000313|EMBL:CCB70548.1,
RC   ECO:0000313|Proteomes:UP000009186};
RX   PubMed=21926215; DOI=10.1128/AEM.05625-11;
RG   1:IP;
RG   Microbial Evolutionary Genomics,F-75015 Paris;
RG   France 2:CNRS;
RG   URA2171;
RG   F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.;
RG   INRA,78352 Jouy en Josas Cedex;
RG   France. 4:Unite de Mathemathique;
RG   Informatique et Genome,INRA;
RG   78352 Jouy en Josas Cedex;
RG   France. 5:CEA/Genoscope;
RG   Evry;
RG   France;
RA   Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., Barbe V.,
RA   Rocha E.P., Duchaud E.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   branchiophilum.";
RL   Appl. Environ. Microbiol. 77:7656-7662(2011).
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}.
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; FQ859183; CCB70548.1; -; Genomic_DNA.
DR   RefSeq; WP_007136545.1; NC_016001.1.
DR   AlphaFoldDB; G2Z459; -.
DR   SMR; G2Z459; -.
DR   STRING; 1034807.FBFL15_2550; -.
DR   KEGG; fbr:FBFL15_2550; -.
DR   eggNOG; COG0361; Bacteria.
DR   HOGENOM; CLU_151267_1_0_10; -.
DR   Proteomes; UP000009186; 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; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000009186};
KW   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   71 AA;  8109 MW;  0E8E9448DBCA4BD9 CRC64;
     MAKQSAIEQD GSIIEALSNA MFRVELENGH IVIAHISGKM RMHYIKLLPG DKVKLEMSPY
     DLSKARITYR Y
//
DBGET integrated database retrieval system