RF3_SYNE7
ID RF3_SYNE7 Reviewed; 556 AA.
AC Q31KM4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Synpcc7942_2365;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; CP000100; ABB58395.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31KM4; -.
DR SMR; Q31KM4; -.
DR STRING; 1140.Synpcc7942_2365; -.
DR PRIDE; Q31KM4; -.
DR EnsemblBacteria; ABB58395; ABB58395; Synpcc7942_2365.
DR KEGG; syf:Synpcc7942_2365; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_3; -.
DR OMA; GFVFKIH; -.
DR BioCyc; SYNEL:SYNPCC7942_2365-MON; -.
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.
FT CHAIN 1..556
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000242221"
FT DOMAIN 28..297
FT /note="tr-type G"
FT BINDING 37..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 105..109
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 159..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ SEQUENCE 556 AA; 63080 MW; DC9344B87C8773C6 CRC64;
MGVHSFLCSS PWFRMVTDLQ KEIQEAVQQR RNFAIISHPD AGKTTLTEKL LLYGGAIQEA
GAVKAKRSQR AATSDWMELE KQRGISITST VLQFNYHDCT INLLDTPGHQ DFSEDTYRTL
AAADNAVMLE DAAKGLEPQT RKLFEVCRMR NIPIFTFFNK MDRPGREPLE LLDEIEQELG
LQTYAVNWPI GSGDRFRGVF DRRKQQVHLF ERSVHGKRQA KDTTLEWGDP QLADLIEPDL
LQQLQDELEL LEGVGTEFDL EAIHAGQLTP VFWGSAMTNF GVELFLEAFL DYALKPGARR
SSVGDMAPDY PEFSGFVFKL QANMDPRHRD RIAFVRVCTG KFEKDMTVQH ARSGRTLRLS
RPQKLFGQDR EVLDDAYPGD VIGLNNPGMF AIGDTIYTGK RLEYDGIPCF SPEIFAYLRN
PNPSKFKPFR KGVSELREEG AVQIMYSADS AKRDPILAAV GQLQLEVVQY RLENEYGVET
LLEPLPFSVA RWVEGGWDVL EKVGRLFNTT TVKDTWGRPV LLFKNEWNLR QIEADHPELQ
LRSVAPVAAG QEPIEV
