ID   RF3_PASMU               Reviewed;         529 AA.
AC   P57879;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Peptide chain release factor 3;
DE            Short=RF-3;
GN   Name=prfC; OrderedLocusNames=PM0816;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02900.1; -; Genomic_DNA.
DR   RefSeq; WP_010906863.1; NC_002663.1.
DR   AlphaFoldDB; P57879; -.
DR   SMR; P57879; -.
DR   STRING; 747.DR93_1656; -.
DR   EnsemblBacteria; AAK02900; AAK02900; PM0816.
DR   KEGG; pmu:PM0816; -.
DR   PATRIC; fig|272843.6.peg.825; -.
DR   HOGENOM; CLU_002794_2_1_6; -.
DR   OMA; GFVFKIH; -.
DR   Proteomes; UP000000809; 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;
KW   Reference proteome.
FT   CHAIN           1..529
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000210953"
FT   DOMAIN          11..280
FT                   /note="tr-type G"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   529 AA;  59517 MW;  48110D3E19B7EE8C CRC64;
     MSLNDYPQQV NKRRTFAIIS HPDAGKTTIT EKVLLYGQAI QTAGSVKGKG SSTHAKSDWM
     EMEKQRGISI TTSVMQFPYN DCLVNLLDTP GHEDFSEDTY RTLTAVDSCL MVIDSAKGVE
     ERTIKLMEVT RLRDTPILTF MNKLDRDIRD PMELLDEVEN VLNIHCAPIT WPIGCGKLFK
     GVYHLYKDET YLYQTGQGHT IQEKRVIKGL DNPELDAAVG DDLAQQLRDE LELVQGASNE
     FDLDAFLQGE LTPVFFGTAL GNFGVDHFLD GLTQWAPAPQ SRQADSRAVA SSEQKLTGFV
     FKIQANMDPK HRDRVAFMRV VSGKYEKGMK LRHVRLGKDV VISDALTFMA GDRSHAEEAY
     AGDIIGLHNH GTIQIGDTFT QGEELKFTGI PNFAPELFRR IRLKDPLKQK QLLKGLVQLS
     EEGAVQVFRP LMNNDLIVGA VGVLQFDVVV SRLKSEYNVE AIYENINVAT ARWVECSDAK
     KFDEFKRKNE QNLALDGGDN LTYIAPTMVN LNLAQERYPD VKFFKTREH