ID   RF3_BUCBP               Reviewed;         532 AA.
AC   Q89A56;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Peptide chain release factor 3;
DE            Short=RF-3;
GN   Name=prfC; OrderedLocusNames=bbp_485;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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 (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; AE016826; AAO27190.1; -; Genomic_DNA.
DR   RefSeq; WP_011091591.1; NC_004545.1.
DR   AlphaFoldDB; Q89A56; -.
DR   SMR; Q89A56; -.
DR   STRING; 224915.bbp_485; -.
DR   EnsemblBacteria; AAO27190; AAO27190; bbp_485.
DR   GeneID; 56471020; -.
DR   KEGG; bab:bbp_485; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_6; -.
DR   OMA; GFVFKIH; -.
DR   OrthoDB; 164090at2; -.
DR   Proteomes; UP000000601; 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..532
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000210935"
FT   DOMAIN          10..283
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   532 AA;  61531 MW;  69FFCF8B3D71D681 CRC64;
     MITINTYALQ KRRTFAIISH PDAGKTTLTE KFLLNGKIIR TSGTIKARRS KKYAKSDWME
     IEKKKGISIT TSVIQIPYNR YLINILDTPG HQDFSEDTYR VLTAVDFCVM IVDAAKGVEE
     RTRKLIHVAR THRTPIITFI NKLDRNSLDP IEILDQLEIE LKIKCSPIIW PISCGKAFKG
     IYHIYNNLVY FYSYKTSEGI NDTNNFLLKT CCLNDVFLDK IIGLELAQEF REEVELVNSI
     YKAFNKRIFL ESDLTPIFFG SALKNFGVNF LMQGILDWAP SPVFKKSNIR KVQPYEKNFS
     GFVFKIQANM DLRHRDRMAF IRIVSGKYRK RMKLYHVRIK KYIIQTEVFS FVAGDRFIIE
     TAYPGDIIGF HSYNSIKIGD TFTEGEKLKF FGIPNFAPEL FRLVSLVDPF HKKKLLKGLT
     QLSEEGAIQV FKPYENNELI LGAIGSLQFD IVIERLKIEY NIFILVHKVN IFSIRWISSN
     SLDTLSTFKN QNKSCLALDI NNHLVYLASS EINLRLVQSR YPDIIFNVTC EN