ID   RF3_SYNY3               Reviewed;         547 AA.
AC   P73473;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Peptide chain release factor 3;
DE            Short=RF-3;
GN   Name=prfC; OrderedLocusNames=slr1228;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17513.1; -; Genomic_DNA.
DR   PIR; S77410; S77410.
DR   AlphaFoldDB; P73473; -.
DR   SMR; P73473; -.
DR   STRING; 1148.1652592; -.
DR   PaxDb; P73473; -.
DR   EnsemblBacteria; BAA17513; BAA17513; BAA17513.
DR   KEGG; syn:slr1228; -.
DR   eggNOG; COG4108; Bacteria.
DR   InParanoid; P73473; -.
DR   OMA; GFVFKIH; -.
DR   PhylomeDB; P73473; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016150; F:translation release factor activity, codon nonspecific; IBA:GO_Central.
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   GO; GO:0006415; P:translational termination; IBA:GO_Central.
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..547
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000210978"
FT   DOMAIN          24..294
FT                   /note="tr-type G"
FT   BINDING         33..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         101..105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..158
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   547 AA;  61189 MW;  90D1B99DC7867004 CRC64;
     MQTSPSSTAP CADKALDDLL KEVDRRRNFA IISHPDAGKT TLTEKLLLYG GAIQEAGAVK
     ARRSQRSATS DWMAMEQQRG ISITSTVLQF DYRGKILNLL DTPGHQDFSE DTYRTLAAAD
     NAVMLIDAAK GLETQTRKLF EVCRLRHLPI FTFINKLDRP SLTPLELMDE IEQELGMNTY
     AVNYPIGTGD RFRGVYNRLT KTIHLFERTG THGSKKAADQ TMALDDPALE SLLGSDVYAE
     FQDELELIEE AGAEFDLAAV HGGEMTPVFF GSAMNNFGVE LFLQAFLQYA AKPEAHDSNR
     GTIEPTYEEF SGFVFKLQAN MDPKHRDRIA FLRVCSGKFE KDMVVKHPRT GKTVRLSRPQ
     KLFAQERESV DIAYAGDVIG LNNPGAFTIG DTVHTGEKII YPPIPSFSPE LFAYLRSTDP
     SQYKNFKKGV SELQEEGAVQ ILQSLDESKR DPILAAVGQL QFEVVQYRLQ EEYGVETRLE
     PLGFSLARWV VEGWDALEKA GRLFNTVVVK DRWDAPVLLF KNQWNLEQVA GDCLDLKLSA
     IAIPPSL