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Database: UniProt
Entry: G7VY10_PAETH
LinkDB: G7VY10_PAETH
Original site: G7VY10_PAETH 
ID   G7VY10_PAETH            Unreviewed;       526 AA.
AC   G7VY10;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
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   OrderedLocusNames=HPL003_02020 {ECO:0000313|EMBL:AET57188.1};
OS   Paenibacillus terrae (strain HPL-003).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=985665 {ECO:0000313|EMBL:AET57188.1, ECO:0000313|Proteomes:UP000005876};
RN   [1] {ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA   Shin S.H., Kim S., Kim J.Y.;
RT   "Complete sequence of Paenibacillus terrae HPL-003.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AET57188.1, ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|EMBL:AET57188.1,
RC   ECO:0000313|Proteomes:UP000005876};
RX   PubMed=22328761; DOI=10.1128/JB.06668-11;
RA   Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA   Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT   "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT   Bacterium Isolated from Soil Found in Forest Residue.";
RL   J. Bacteriol. 194:1266-1266(2012).
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; CP003107; AET57188.1; -; Genomic_DNA.
DR   RefSeq; WP_014277971.1; NC_016641.1.
DR   AlphaFoldDB; G7VY10; -.
DR   STRING; 985665.HPL003_02020; -.
DR   KEGG; pta:HPL003_02020; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_9; -.
DR   OMA; GFVFKIH; -.
DR   OrthoDB; 9801591at2; -.
DR   Proteomes; UP000005876; 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   CDD; cd03689; RF3_II; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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   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; 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}.
FT   DOMAIN          13..281
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         22..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         90..94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   526 AA;  59661 MW;  80A9C989C40272B3 CRC64;
     MSKTLDILQQ EVDKRRTFAI ISHPDAGKTT LTEKLLLFGG AIRLAGSVKA RKASKHATSD
     WMEIEKQRGI SVTSSVMQFD YNGHRINILD TPGHQDFSED TYRTLTAADS AVMLIDVAKG
     VEAQTIKLFQ VCAKRGIPIF TFINKLDREG RSPFDLMEEL EQVLGIRSVP MNWPIGTGRE
     LCGVYDRVKN QVELFQGDDH STIKVQKVED YNDPIIREMA GEYLHDQLCQ DLELLDVAGD
     PFDMEKVQRG ELTPVFFGSA INNFGVQTFL ENFLQLAPKP EPRRSTAGEI EPTNEKFTGY
     VFKIQANMNP AHRDRIAFLR IVSGKFQRGM SVKHVRMGKE IKLSQPQQFL AQDRDIVEEA
     FPGDIIGLFD PGIFRIGDSL SQGGEVVFDE LPTFSPEIFA KVTVKNALKH KQYLKGIDQL
     TEEGMIQVFR TVSFDDTLLG VVGQLQFEVF EYRMKGEYGV DVQLQRMPFQ FARWIVDDQI
     DPSKFRINST LVKDKKGNYV ALFENEYAMR TAIEKNPTAK FLEMAP
//
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