IF3_DEIDV
ID IF3_DEIDV Reviewed; 210 AA.
AC C1D0V9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=Deide_06380;
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO45483.1; -; Genomic_DNA.
DR RefSeq; WP_012692606.1; NC_012526.1.
DR AlphaFoldDB; C1D0V9; -.
DR SMR; C1D0V9; -.
DR STRING; 546414.Deide_06380; -.
DR PaxDb; C1D0V9; -.
DR EnsemblBacteria; ACO45483; ACO45483; Deide_06380.
DR KEGG; ddr:Deide_06380; -.
DR eggNOG; COG0290; Bacteria.
DR HOGENOM; CLU_054919_3_1_0; -.
DR OMA; RNMIMFL; -.
DR OrthoDB; 1760144at2; -.
DR Proteomes; UP000002208; 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..210
FT /note="Translation initiation factor IF-3"
FT /id="PRO_1000202538"
FT REGION 169..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23567 MW; 5A013E52C26A1714 CRC64;
MINIAKEHKV NEQIRVRQIR LIGGEGEQIG IIDTRDAMNM AREKGLDLVM VSPQAVPPVC
RLLDYGRFRY EQQQNEKENR KRVRSQEVKA IKFRVKIDDH DFKTKTGHVR RFLDDGHKVK
VTIMFRGRER THPELGERIL VRVAEALADV GTPEGMPSMM GMDMNMIMAP KQAPAPKKER
TEESAEKAGS AGETEPVPAA SAAAEAPANV
