RF3_SHESH
ID RF3_SHESH Reviewed; 526 AA.
AC A8FYR3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Ssed_3382;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) 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; CP000821; ABV37986.1; -; Genomic_DNA.
DR RefSeq; WP_012143716.1; NC_009831.1.
DR AlphaFoldDB; A8FYR3; -.
DR SMR; A8FYR3; -.
DR STRING; 425104.Ssed_3382; -.
DR EnsemblBacteria; ABV37986; ABV37986; Ssed_3382.
DR KEGG; sse:Ssed_3382; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_6; -.
DR OMA; GFVFKIH; -.
DR OrthoDB; 164090at2; -.
DR Proteomes; UP000002015; 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; 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.
FT CHAIN 1..526
FT /note="Peptide chain release factor 3"
FT /id="PRO_1000075170"
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; 59148 MW; C268314D39EA5261 CRC64;
MSGNKVEVDK RRTFAIISHP DAGKTTITEK VLLFGNALQK AGTVKGKKSG QHAKSDWMEM
EKDRGISITT SVMQFPYNGA LVNLLDTPGH EDFSEDTYRT LTAVDSCLMV IDSAKGVEQR
TIKLMEVTRL RDTPIVTFMN KLDRDIRDPL ELMDEVEKVL NIACAPITWP IGCGKEFKGV
YHLLRDEVIL YQSGQGHTIQ DSTIIKGLDN PELDAAIGTY AAEVREELEL VLGASNEFDL
ELFLAGELTP VYFGTALGNF GVDHILDGIV EWAPKPQARE TEVREVQPED EKFSGFVFKI
QANMDPKHRD RVAFMRVCSG RYEQGMKMHH VRLGKDVNVS DALTFMAGDR NRAEVAYPGD
IIGLHNHGTM RIGDTFTQGE KLRFTGIPNF APEMFRRIRL KDPLKQKQLL KGLVQLSEEG
AVQVFRPIDT NDLIVGAVGI LQFEVVVGRL KSEYKVEAIY EAISVSTARW VYCDDERKLE
EFRRKCSTNL ALDGGDNLTY IAPTMVNLNL SMERYPDIKF AKTREN