ID A0A3G9J2D3_9BACL Unreviewed; 528 AA.
AC A0A3G9J2D3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:BBH24722.1};
GN ORFNames=Back11_60670 {ECO:0000313|EMBL:BBH24722.1}, FHS14_005153
GN {ECO:0000313|EMBL:MBB3072138.1};
OS Paenibacillus baekrokdamisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1712516 {ECO:0000313|EMBL:BBH24722.1, ECO:0000313|Proteomes:UP000275368};
RN [1] {ECO:0000313|EMBL:BBH24722.1, ECO:0000313|Proteomes:UP000275368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33723 {ECO:0000313|EMBL:BBH24722.1,
RC ECO:0000313|Proteomes:UP000275368};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Lee J.S.;
RT "Complete genome sequence of Paenibacillus baekrokdamisoli strain KCTC
RT 33723.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3072138.1, ECO:0000313|Proteomes:UP000562277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8890 {ECO:0000313|EMBL:MBB3072138.1,
RC ECO:0000313|Proteomes:UP000562277};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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; AP019308; BBH24722.1; -; Genomic_DNA.
DR EMBL; JACHXC010000014; MBB3072138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9J2D3; -.
DR KEGG; pbk:Back11_60670; -.
DR OrthoDB; 9801591at2; -.
DR Proteomes; UP000275368; Chromosome.
DR Proteomes; UP000562277; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000275368}.
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 528 AA; 59898 MW; 9B82094303C5670E CRC64;
MSKPITDEIK QEVEKRRTFA IISHPDAGKT TLTEKLLLFG GAIREAGTVK ARKANRHATS
DWMEIEKQRG ISVTSSVMQF DYSGHRINIL DTPGHQDFSE DTYRTLTAAD SAVMLIDVAK
GVEAQTIKLF QVCRKRGIPI FTFINKLDRE GQSPFELMEE LERVLGIRAV PMNWPIGMGR
ELCGVYDRMK NQVELFKGND HSTISVQKVT DYNDTVIREM AGDYLHDQLV QDLELLDVAG
DQFDFDKVRA GELTPLFFGS AVNNFGVQTF LENFLQLAPS PTPRNSTTGL IDPMSDKFTG
YVFKIQANMN PAHRDRIAFL RICSGRFERG MSVRHVRAGK DIKLSQPQQF LAQDRDIVES
AYPGDIIGLF DPGIFRIGDS LSQGGEVIFD ELPTFSPEIF AKVTVKNALK YKQYQKGINQ
LTEEGTIQVF HSSGGFDETI LGVVGHLQFE VFEYRMRAEY GVEIQLHRMT FQFARWIVDD
KIDPSKYRIN STLVKDKKDN YVALFENEYA MRTAMEKNPT SKFLETAP
//
