ID   IF3_SYNPW               Reviewed;         220 AA.
AC   A5GI06;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN   Name=infC {ECO:0000255|HAMAP-Rule:MF_00080};
GN   OrderedLocusNames=SynWH7803_0145;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the
CC       equilibrum between 70S ribosomes and their 50S and 30S subunits in
CC       favor of the free subunits, thus enhancing the availability of 30S
CC       subunits on which protein synthesis initiation begins.
CC       {ECO:0000255|HAMAP-Rule:MF_00080}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00080}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00080}.
CC   -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00080}.
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; CT971583; CAK22571.1; -; Genomic_DNA.
DR   RefSeq; WP_011932079.1; NC_009481.1.
DR   AlphaFoldDB; A5GI06; -.
DR   SMR; A5GI06; -.
DR   STRING; 32051.SynWH7803_0145; -.
DR   EnsemblBacteria; CAK22571; CAK22571; SynWH7803_0145.
DR   KEGG; syx:SynWH7803_0145; -.
DR   eggNOG; COG0290; Bacteria.
DR   HOGENOM; CLU_054919_3_1_3; -.
DR   OMA; RNMIMFL; -.
DR   OrthoDB; 1760144at2; -.
DR   Proteomes; UP000001566; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.20.80; -; 1.
DR   Gene3D; 3.30.110.10; -; 1.
DR   HAMAP; MF_00080; IF_3; 1.
DR   InterPro; IPR036788; T_IF-3_C_sf.
DR   InterPro; IPR036787; T_IF-3_N_sf.
DR   InterPro; IPR019813; Translation_initiation_fac3_CS.
DR   InterPro; IPR001288; Translation_initiation_fac_3.
DR   InterPro; IPR019815; Translation_initiation_fac_3_C.
DR   InterPro; IPR019814; Translation_initiation_fac_3_N.
DR   PANTHER; PTHR10938; PTHR10938; 1.
DR   Pfam; PF00707; IF3_C; 1.
DR   Pfam; PF05198; IF3_N; 1.
DR   SUPFAM; SSF54364; SSF54364; 1.
DR   SUPFAM; SSF55200; SSF55200; 1.
DR   TIGRFAMs; TIGR00168; infC; 1.
DR   PROSITE; PS00938; IF3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..220
FT                   /note="Translation initiation factor IF-3"
FT                   /id="PRO_1000004581"
FT   REGION          182..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   220 AA;  25346 MW;  513AFDCE81DD8A52 CRC64;
     MPPRPRFDRR APVRELPNIN ERINYPQLRV VDADGTQLGV IDREKALEVA QERELDLVLV
     SEKADPPVCR IMDYGKYKFE QEKKAKEAKK KSHQTEVKEV KMRYKIDQHD YDVRIGQAQR
     FLKAGDKVKC TVIFRGREIQ HTALAETLLR RMAKDLEEPA EIQQPPKREG RNMIMFLTPR
     KTPLVKKDDK EEPATRAVRT ITAPPRPTSA RLASKPAGNG