ID   RF3_BUCAT               Reviewed;         526 AA.
AC   B8D867;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Peptide chain release factor 3 {ECO:0000255|HAMAP-Rule:MF_00072};
DE            Short=RF-3 {ECO:0000255|HAMAP-Rule:MF_00072};
GN   Name=prfC {ECO:0000255|HAMAP-Rule:MF_00072};
GN   OrderedLocusNames=BUAPTUC7_537;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
CC   -!- FUNCTION: Increases the formation of ribosomal termination complexes
CC       and stimulates activities of RF-1 and RF-2. It binds guanine
CC       nucleotides and has strong preference for UGA stop codons. It may
CC       interact directly with the ribosome. The stimulation of RF-1 and RF-2
CC       is significantly reduced by GTP and GDP, but not by GMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00072}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00072}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00072}.
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DR   EMBL; CP001158; ACL30332.1; -; Genomic_DNA.
DR   RefSeq; WP_012619577.1; NC_011834.1.
DR   AlphaFoldDB; B8D867; -.
DR   SMR; B8D867; -.
DR   KEGG; bau:BUAPTUC7_537; -.
DR   HOGENOM; CLU_002794_2_1_6; -.
DR   OMA; GFVFKIH; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-UniRule.
DR   CDD; cd04169; RF3; 1.
DR   Gene3D; 3.30.70.3280; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00072; Rel_fac_3; 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004548; PrfC.
DR   InterPro; IPR032090; RF3_C.
DR   InterPro; IPR038467; RF3_dom_3_sf.
DR   InterPro; IPR041732; RF3_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43556; PTHR43556; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF16658; RF3_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 1.
DR   TIGRFAMs; TIGR00503; prfC; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..526
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_1000193516"
FT   DOMAIN          11..277
FT                   /note="tr-type G"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   526 AA;  60285 MW;  C916D841E20DD2D5 CRC64;
     MFDSNHEQEL SKRRTFAIIS HPDAGKTTIT EKMLFFGKVI RVPGTIKGRG SGKYAKSDWM
     NIEKERGISI TTSVMQFTYK NILMNLLDTP GHQDFSEDTY RILTAVDCCL VVIDAAKGIE
     ERTRKLMDVA RIHNTPIITF INKLDRDSRD PIEILDEIEK ELKLHCIPIS WPISCGKNFR
     GVYHIHDKII HLYKSKFRKN FLTLDSFLDG SLNEYLGADL SIYIRQELEL IMNVYSKFNK
     EKFLKGITTP IFFGSALGNF GIDHLLDSLI KWAPSPLYRQ SNKRIIKPQE RNFTGFIFKI
     QANMDLKHRD RIAFMRIVSG QYTKGMKLTH VRIKKNIIIS DAFSFLAGER ISINKAYPGD
     VIGLHNHGTI KIGDTFTQGE EIKFIGIPSF APEIFRLIYL KNPLKQKQLK KGLVQLSEEG
     TVQVFRPILN NDLILGAIGI LQFDVVIERL RIEYNIDAVY KKVNIVLARW INCGNHHSLY
     NLKKSYSSYL AYDISNSLIY LAPSSANLNI VMSQNSDISF NATREQ