ID   RF3_BUCAI               Reviewed;         526 AA.
AC   P57608;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Peptide chain release factor 3;
DE            Short=RF-3;
GN   Name=prfC; OrderedLocusNames=BU543;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BA000003; BAB13235.1; -; Genomic_DNA.
DR   RefSeq; NP_240349.1; NC_002528.1.
DR   RefSeq; WP_010896156.1; NC_002528.1.
DR   AlphaFoldDB; P57608; -.
DR   SMR; P57608; -.
DR   STRING; 107806.10039201; -.
DR   EnsemblBacteria; BAB13235; BAB13235; BAB13235.
DR   KEGG; buc:BU543; -.
DR   PATRIC; fig|107806.10.peg.547; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_6; -.
DR   OMA; GFVFKIH; -.
DR   Proteomes; UP000001806; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..526
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000210933"
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:0000250"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  60359 MW;  87FD35127309C04B CRC64;
     MFDSNHEQEL SKRRTFAIIS HPDAGKTTIT EKMLFFGKVI RVPGTIKGRG SGKYAKSDWM
     NIEKERGISI TTSVMQFTYK NILMNLLDTP GHQDFSEDTY RILTAVDCCL VVIDAAKGIE
     ERTRKLMDVA RIHNTPIITF INKLDRDSRD PIEILDEIEK ELKLHCIPIS WPISCGKNFR
     GVYHIYDKII HLYKSKFRKN FLTLDSFLDG SLNEYLGADL SIHIRQELEL IMNVYSKFNK
     EKFLKGITTP IFFGSALGNF GIDHLLDSLI KWAPSPLYRQ SNKRIIKPQE RKFTGFIFKI
     QANMDLKHRD RIAFMRIVSG QYTKGMKLTH VRIKKNIIIS DAFSFLAGER ISINKAYPGD
     VIGLHNHGTI KIGDTFTQGE EIKFIGIPSF APEIFRLIYL KNPLKQKQLK KGLVQLSEEG
     TVQVFRPILN NDLILGAIGI LQFDVVIERL RIEYNIDAVY KKVNIVLARW INYGNHHSLY
     NLKKSYSSYL AYDISNSLIY LAPSSANLNI VMSQNSDISF NATREQ