ID   RF3_GEOSL               Reviewed;         526 AA.
AC   Q74GV6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=GSU0138;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR33473.1; -; Genomic_DNA.
DR   RefSeq; NP_951200.1; NC_002939.5.
DR   RefSeq; WP_010940814.1; NC_002939.5.
DR   AlphaFoldDB; Q74GV6; -.
DR   SMR; Q74GV6; -.
DR   STRING; 243231.GSU0138; -.
DR   EnsemblBacteria; AAR33473; AAR33473; GSU0138.
DR   KEGG; gsu:GSU0138; -.
DR   PATRIC; fig|243231.5.peg.139; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_7; -.
DR   InParanoid; Q74GV6; -.
DR   OMA; TPASWPI; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016150; F:translation release factor activity, codon nonspecific; IBA:GO_Central.
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   GO; GO:0006415; P:translational termination; IBA:GO_Central.
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..526
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000242180"
FT   DOMAIN          9..277
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         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   526 AA;  59537 MW;  D6EE68E9EA8F7906 CRC64;
     MKYNEQEVDR RRTFAIVSHP DAGKTTITEK LLLFGGAIQQ AGEVRARKAA RHATSDWMEM
     EKQRGISVTS SVMKFTYRDY EVNLLDTPGH NDFSEDTYRV LTAVDSALMV IDSVKGVESQ
     TIKLLDVCRL RHTPIMTFIN KLDREGRDPF ELIDEIEKVL RIQCAPMTWP IGMGKRFRGT
     YHLYTKELVI FDAEAERGTG GVISMTGLDD PQLDELLGSQ ADELRADVEL LEGAAHPFEE
     EAYHAGLQTP VFFGSAINTF GVQQLLDTFV DHAPAPLPRE AVSRTVSPYE EPFTAFAFKI
     QANMDPAHRD RIAFFRICSG KFTRGMKVRH VRLGREVAIN NATIFMAQDR THVDEAFPGD
     IIGIHNHGTI KIGDTFTLGE DIKFTGIPNF APEHFRRVRL LDPLKSKALE KGLTQLAEEG
     TTQVFRPLMG ADWVVGAVGL LQFDVVMHRL EHEYNVKATY EPVSYVTARW VTGEKKKVEE
     FQKKEVMNCY IDGEGDLAYL AGSQWRLDNT MDNWKDLTFH ATREHS