ID   RF3_MICAN               Reviewed;         544 AA.
AC   B0JIY7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=MAE_58730;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009552; BAG05695.1; -; Genomic_DNA.
DR   RefSeq; WP_012268066.1; NC_010296.1.
DR   AlphaFoldDB; B0JIY7; -.
DR   SMR; B0JIY7; -.
DR   STRING; 449447.MAE_58730; -.
DR   PaxDb; B0JIY7; -.
DR   EnsemblBacteria; BAG05695; BAG05695; MAE_58730.
DR   KEGG; mar:MAE_58730; -.
DR   PATRIC; fig|449447.4.peg.5378; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_3; -.
DR   OMA; GFVFKIH; -.
DR   OrthoDB; 164090at2; -.
DR   BioCyc; MAER449447:MAE_RS25635-MON; -.
DR   Proteomes; UP000001510; 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..544
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_1000075163"
FT   DOMAIN          17..286
FT                   /note="tr-type G"
FT   BINDING         26..33
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         94..98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         148..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   544 AA;  61499 MW;  D7C7FA2B0F848E4E CRC64;
     MTTEIEKELE TSEAVLEKRR NFAIISHPDA GKTTLTEKLL LYGGAIHQAG AVKARRDQRK
     ATSDWMEMEK QRGISITSTV LQFDYRDFQI NLLDTPGHQD FSEDTYRTLA AADNAVMLID
     AAKGLEPQTR KLFEVCKLRQ LPIFTFVNKM DRPGREPLDL LDEIERELGL QTYPVNWPIG
     IGDRFRGVFD RATQTIHLFE RRSHGSQEAQ ETVIELGDPK IEDYLEKDLY YQLKEDIELL
     SELGAELDLP AVHAGEMTPI FFGSAMTNFG VKLFLESFLD YGLAPRGRNS SLGVLDPTYP
     DFTGFVFKLQ ANMDPKHRDR VAFVRVCTGK FEKDMVVNHA RTGKTIRLSR PQKLFAQDRA
     VIEEAYPGDV IGLNNPGVFA IGDTIYMGKK LEYEGIPCFS PELFAYLRNP NPSKFKQFQK
     GVSELQEEGA VQILSSIDEF KRDPILAAVG QLQFEVVQFR LLSEYGVETT LEPLAYSLAR
     WVAGGWAALE KAGKLFNTLT VKDYWGRPVL LFKNEWNLQQ VKEDHPSLQL NSIAPVGSGV
     QPQS