ID   RF3_SHEB2               Reviewed;         526 AA.
AC   B8E6N9;
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=Sbal223_1135;
OS   Shewanella baltica (strain OS223).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=407976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS223;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA   Tiedje J.;
RT   "Complete sequence of chromosome of Shewanella baltica OS223.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001252; ACK45650.1; -; Genomic_DNA.
DR   RefSeq; WP_012587035.1; NC_011663.1.
DR   AlphaFoldDB; B8E6N9; -.
DR   SMR; B8E6N9; -.
DR   EnsemblBacteria; ACK45650; ACK45650; Sbal223_1135.
DR   KEGG; sbp:Sbal223_1135; -.
DR   HOGENOM; CLU_002794_2_1_6; -.
DR   OMA; GFVFKIH; -.
DR   Proteomes; UP000002507; 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; -; 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.
FT   CHAIN           1..526
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_1000193534"
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;  59234 MW;  393CF8DF66A38A21 CRC64;
     MSGNKVEVDK RRTFAIISHP DAGKTTITEK VLLFGNALQK AGTVKGKKSG QHAKSDWMEM
     EKDRGISITT SVMQFPYGGA LVNLLDTPGH EDFSEDTYRT LTAVDSCLMV IDSAKGVEER
     TIKLMEVTRL RDTPIVTFMN KLDRDIRDPI DLMDEVESVL NIACAPITWP IGSGKEFKGI
     YHILRDEVVL YQGGMGHTIQ DRRVIKGINN PDLEKAIGSY AADLRDEMEL VRGASHEFDH
     AAFLKGELTP VFFGTALGNF GVDHILDGIV EWAPKPLPRE SDARVVMPEE EKFTGFVFKI
     QANMDPKHRD RVAFMRVCSG RYEQGMKMHH VRIGKDVNVS DALTFMAGDR ERAEEAYPGD
     IIGLHNHGTI RIGDTFTQGE KFRFTGVPNF APEMFRRIRL RDPLKQKQLL KGLVQLSEEG
     AVQVFRPIDT NDLIVGAVGV LQFEVVVGRL KSEYNVEAIY EGISVSTARW VYCKDERKLE
     EFRRKCSQNL ALDGGDNLTY IAPTMVNLNL SMERYPDIEF AKTREH