ID   RF3_DICNO               Reviewed;         531 AA.
AC   P39883;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Peptide chain release factor 3;
DE            Short=RF-3;
GN   Name=prfC;
OS   Dichelobacter nodosus (Bacteroides nodosus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A198;
RX   PubMed=7539688; DOI=10.1099/13500872-141-4-945;
RA   Billington S.J., Jost B.H., Rood J.I.;
RT   "A gene region in Dichelobacter nodosus encoding a lipopolysaccharide
RT   epitope.";
RL   Microbiology 141:945-957(1995).
CC   -!- FUNCTION: Increases the formation of ribosomal termination complexes
CC       and stimulates activities of RF-1 and RF-2. It binds guanine
CC       nucleotides but is not codon-specific. It may interact directly with
CC       the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced
CC       by GTP and GDP, but not by GMP (By 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U06471; AAC43387.1; -; Genomic_DNA.
DR   RefSeq; WP_012030836.1; NZ_SRJB01000010.1.
DR   AlphaFoldDB; P39883; -.
DR   SMR; P39883; -.
DR   PRIDE; P39883; -.
DR   PATRIC; fig|870.4.peg.879; -.
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; 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.
FT   CHAIN           1..531
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000210929"
FT   DOMAIN          10..279
FT                   /note="tr-type G"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         87..91
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   531 AA;  59960 MW;  82E55EADB0178877 CRC64;
     MSDILSQDWR DRRTFAIISH PDAGKTTLTE KLLLFGGAIA LAGAVKGRKA AHHATSDWMK
     MEQERGISVT SSVMQFPYHG KVINLLDTPG HEDFSEDTYR TLTAVDSALM VIDCAKGVEE
     RTIKLMEVCR LRTTPIFTFV NKLDRDGREP MEILDEIERV LHIQCAPVTW PIGMGRSLKG
     IYHLARDTVY FYTTGKGGAS INHGETVVGL DNPRLDTLLP DIIDDFREEI HFLREVGNPF
     DHEAYLRGEL TPVYFGSAIS NFGVEEMLTD FAQLAPPPRP HRTTEREVAP QEEKLTGFVF
     KIQANMDLKH RDRIAFMRVN SGTFRAGMKL WQVRLGREVK IPDALTFLAA EREHAQEAFA
     GDIIGIHNHG TIRIGDTFTE GESLQFTGIP DFAPELFRRV QLKDPLKMKA LLKGLAQLCE
     EGATQFFKPL IGSDLILGAI GVLQFEVVQQ RLETEYNVKC QFESVAVATA RWIEAPNDKA
     LKQFIDKNQA NLAHDHYEQL VYIAPSRVNL QLTQERFPDI VFSQTRDHLA Q