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IF3_LEPIN
ID   IF3_LEPIN               Reviewed;         179 AA.
AC   Q8F6Q9;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN   Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=LA_1242;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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}.
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DR   EMBL; AE010300; AAN48441.1; -; Genomic_DNA.
DR   RefSeq; NP_711423.1; NC_004342.2.
DR   RefSeq; WP_001189133.1; NC_004342.2.
DR   AlphaFoldDB; Q8F6Q9; -.
DR   SMR; Q8F6Q9; -.
DR   STRING; 189518.LA_1242; -.
DR   EnsemblBacteria; AAN48441; AAN48441; LA_1242.
DR   GeneID; 61142340; -.
DR   KEGG; lil:LA_1242; -.
DR   PATRIC; fig|189518.3.peg.1243; -.
DR   HOGENOM; CLU_054919_3_2_12; -.
DR   InParanoid; Q8F6Q9; -.
DR   OMA; RNMIMFL; -.
DR   PRO; PR:Q8F6Q9; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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..179
FT                   /note="Translation initiation factor IF-3"
FT                   /id="PRO_0000177535"
SQ   SEQUENCE   179 AA;  20776 MW;  3C82FEDB3AB10AF9 CRC64;
     MQRKPSQKSA TDKLFNHRVN EKITGVSRVR LVSDDGVAIV SFEEALRKAK EENLDLVEVS
     ADQELHVCKI IDYGKYKFEL LKKSKEAKKK QHVINVKEIK IRPRIESHDY EIKKKHAQEF
     LGKGDKVKVS LRFRGREMMH SDLGMKVVYR MIEDLKEHGT AERDPIQDGK QIVVIINPK
 
 
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