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Database: UniProt
Entry: G3IRG6_METTV
LinkDB: G3IRG6_METTV
Original site: G3IRG6_METTV 
ID   G3IRG6_METTV            Unreviewed;       531 AA.
AC   G3IRG6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Peptide chain release factor 3 {ECO:0000256|HAMAP-Rule:MF_00072};
DE            Short=RF-3 {ECO:0000256|HAMAP-Rule:MF_00072};
GN   Name=prfC {ECO:0000256|HAMAP-Rule:MF_00072};
GN   ORFNames=Mettu_0978 {ECO:0000313|EMBL:EGW22177.1};
OS   Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylobacter.
OX   NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW22177.1, ECO:0000313|Proteomes:UP000004664};
RN   [1] {ECO:0000313|EMBL:EGW22177.1, ECO:0000313|Proteomes:UP000004664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1195 / DSM 17260 / SV96
RC   {ECO:0000313|Proteomes:UP000004664};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Held B.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Klotz M.G., Dispirito A.A., Murrell J.C.,
RA   Dunfield P., Kalyuzhnaya M.G., Svenning M., Trotsenko Y.A., Stein L.Y.,
RA   Woyke T.;
RT   "Genomic sequence of Methylobacter tundripaludum SV96.";
RL   Submitted (JUN-2011) 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:0000256|HAMAP-Rule:MF_00072}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|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:0000256|ARBA:ARBA00009978, ECO:0000256|HAMAP-Rule:MF_00072}.
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DR   EMBL; JH109152; EGW22177.1; -; Genomic_DNA.
DR   RefSeq; WP_006890152.1; NZ_JH109152.1.
DR   AlphaFoldDB; G3IRG6; -.
DR   STRING; 697282.Mettu_0978; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_6; -.
DR   OMA; GFVFKIH; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000004664; Unassembled WGS sequence.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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   CDD; cd03689; RF3_II; 1.
DR   CDD; cd16259; RF3_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 1.
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   NCBIfam; TIGR00503; prfC; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43556; PEPTIDE CHAIN RELEASE FACTOR RF3; 1.
DR   PANTHER; PTHR43556:SF2; PEPTIDE CHAIN RELEASE FACTOR RF3; 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; SSF54980; EF-G C-terminal domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00072};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00072};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00072}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004664}.
FT   DOMAIN          14..282
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         23..30
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         145..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   531 AA;  59658 MW;  3FF41F1EC63E1E03 CRC64;
     MNELLNSLQV RETRRRRTFA IISHPDAGKT TITEKLLLFG GAIQLAGSVK GRKAARHATS
     DWMEMEKERG ISVTTSVMQF EHKDCIINLL DTPGHEDFSE DTYRTLTAVD SALMVIDVAK
     GVEDRTINLM EVCRLRTTPI LTFINKLDRE GREPIELMDE VENVLNIKCA PMTWPIGMGK
     RFKGVYHLYK DEIHLFSAQH GGKIAQAEII KGLDNPKLDE LLDDQAEELR DEIDLVKGAS
     HEFDLEEYLA GKLTPVFFGS AINNFGIIEL LDAFAEYAPS PRPREAEQRT VLPDEPAFSG
     FVFKVQANMD PSHRDRIAFL RVCSGKFDKG MKVHHVRIGK NIQVANAITF QADSRKSVEE
     AYPGDIIGLH NHGTIQVGDT FTQGETLKYG GIPYFAPELF RRVVLKDPLR AKALQKGLVQ
     LTEEGATQLF KPLKNNDLIL GAVGVLQFDV TAFRLKSEYN VECVYDAVPI SAVRWVSSDK
     PAKLEEFKNK AFDNLAEDGG GYLVYVANSR VNLQLTEERW PDIKFSATRE L
//
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