ID   RF3_CUPNH               Reviewed;         533 AA.
AC   Q0JY21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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}; OrderedLocusNames=H16_B2571;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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; AM260480; CAJ97353.1; -; Genomic_DNA.
DR   RefSeq; WP_010811156.1; NZ_CP039288.1.
DR   AlphaFoldDB; Q0JY21; -.
DR   SMR; Q0JY21; -.
DR   STRING; 381666.H16_B2571; -.
DR   EnsemblBacteria; CAJ97353; CAJ97353; H16_B2571.
DR   GeneID; 57648467; -.
DR   KEGG; reh:H16_B2571; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_4; -.
DR   OMA; GFVFKIH; -.
DR   OrthoDB; 164090at2; -.
DR   Proteomes; UP000008210; Chromosome 2.
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; -; 2.
DR   HAMAP; MF_00072; Rel_fac_3; 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..533
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_1000023673"
FT   DOMAIN          9..284
FT                   /note="tr-type G"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         95..99
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         149..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   533 AA;  59314 MW;  0481A7E6B7AFA7B3 CRC64;
     MSSLVSEIAR RRTFAIISHP DAGKTTLTEK LLWFGGAIQV AGEVRARKAD RHATSDWMEL
     EKQRGISVTS SVMQFPYRRE TADGKAQENI VNLLDTPGHE DFSEDTYRTL TAVDSAVMVI
     DSVNGVEAQT IKLLNVCRLR DTPILTFINK LDREGRSPIE LLDEIEEVLQ IQCAPMTWPI
     GMGKAFRGVY HLINDKVQLF DPHGEKGTAA ILDGLDNPEL DRILGSQAEE LRIEIELVRG
     ASHTFDKDAF LNGKQTPVYF GSAINNFGVQ SLLDALCELS PPPLARNTDS RVVEPQEPKF
     TGFVFKIQAN MDPRHRDRIA FVRVCSGRFE RGMKLLHVSA GKTVAINNAI TFMAQDRNTT
     EEAYAGDIIG VPNHGTIRLG DVFTEGEPLK FTGIPSFAPE FFRRARLNNP LKVKQLQKGL
     QQLAEEGATQ MFRPLASNDL VLGAVGILQF DVVAHRLEHE YGVDAIFESH ECATARWLKG
     TPAEIEKLIA KAGHNVALDG AGDHVYLAPS MVNLRLTQER FPELQFMETR EIV