ID A0A191TJW7_9BACT Unreviewed; 527 AA.
AC A0A191TJW7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=A9P82_06655 {ECO:0000313|EMBL:ANI89002.1};
OS Arachidicoccus sp. BS20.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=1850526 {ECO:0000313|EMBL:ANI89002.1, ECO:0000313|Proteomes:UP000078308};
RN [1] {ECO:0000313|EMBL:ANI89002.1, ECO:0000313|Proteomes:UP000078308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS20 {ECO:0000313|EMBL:ANI89002.1,
RC ECO:0000313|Proteomes:UP000078308};
RA Im W.T., Siddiqi M.Z.;
RT "Arachidicoccus sp. BS20 whole genome sequincing.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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; CP015971; ANI89002.1; -; Genomic_DNA.
DR RefSeq; WP_066205707.1; NZ_CP015971.1.
DR AlphaFoldDB; A0A191TJW7; -.
DR STRING; 1850526.A9P82_06655; -.
DR KEGG; arb:A9P82_06655; -.
DR OrthoDB; 9801591at2; -.
DR Proteomes; UP000078308; 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; 3.40.50.300; 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; 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:UP000078308}.
FT DOMAIN 8..276
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 527 AA; 60137 MW; F4CD86A1399E09D6 CRC64;
MSYEKEISRR KSFAIISHPD AGKTTLTEKL LLFGGAIQTA GAVKSNKIKK HATSDFMEIE
RQRGISVATS VMTFEYKDFL INLLDTPGHK DFAEDTYRTL TAVDSVILVV DSVNGVEDQT
RRLMEVCRMR DTPVIVFINK MDRDGKNRFD LLEEIEKELK IDLHPMTLPI NSGKDFKGVY
NLHDKNLLLF TANTKADEDS VEIKDLNNEI LSQKIGESDA NTLREDVELV DGVYGELNVE
DYLSGKTAPV FFGSAVNNFG VKEMLDTFIR IAPNPQHRET TTRIVEPNEE KFSGFVFKIH
ANLDPKHRDR IAFLRVCSGK FERGKYYEHV RLDKDIRFNN PYSFLARSKD IIEDAYPGDV
IGLFDTGNFK IGDTLTEGEK FYFTGIPSFS PEIFKELVNK DPMKTKQMEK GVAQLTDEGV
AQLFTQFGGN KKIIGCVGEL QFEVIQYRLL QEYGAAVEFR TLPFYKACWL TSESPKTLED
FLRFKQQNAA EDKDGNPVYL AQSEWFLNTE ITNNPDIQFH FTSEIHK
//
