ID A0A368JS28_9BACT Unreviewed; 531 AA.
AC A0A368JS28;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=DUE52_05800 {ECO:0000313|EMBL:RCR70467.1};
OS Larkinella punicea.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Larkinella.
OX NCBI_TaxID=2315727 {ECO:0000313|EMBL:RCR70467.1, ECO:0000313|Proteomes:UP000253383};
RN [1] {ECO:0000313|EMBL:RCR70467.1, ECO:0000313|Proteomes:UP000253383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zzj9 {ECO:0000313|Proteomes:UP000253383};
RA Zhou Z., Wang G.;
RT "Genome analysis of Larkinella rosea.";
RL Submitted (JUL-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCR70467.1}.
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DR EMBL; QOWE01000004; RCR70467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368JS28; -.
DR OrthoDB; 9801591at2; -.
DR Proteomes; UP000253383; 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; cd16259; RF3_III; 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 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 531 AA; 60466 MW; 1DEE905A6E7D519A CRC64;
MSTTQEISRR RTFAIISHPD AGKTTLTEKL LLFGGAIQTA GAVKSNKIKK SATSDFMEIE
KQRGISVATS VMTFEYKDLK INILDTPGHK DFAEDTYRTL TAVDSVILVI DCVKGVEEQT
ERLMEVCRMR DTPVIIFINK LDREGQDPFD LLDELESKLN LRVRPLTWPV NMGSDFKGVY
SLYDKTMNFF RINKTKVEED ILEIDITTPV LEQKVGERDA EQLREDAELI EGIYDPFDRQ
TYLEGKVAPV FFGSAVNNFG VKELLDTFCS ISPEPIARAT DKRVVFPDEP KFTGFVFKIH
ANLDPRHRDR IAFLRICSGV FERGKFYHHT RLDKDVRFSS PFSFMADSKS IVDEGFPGDV
VGLYDTGSFK IGDTLTEGED MRYVGIPSFS PEIFKELINS DPMKSKQLEK GIQQLTDEGV
AQLFTMMSGN RKIVGTVGEL QFDVIQYRLE HEYGAKCRWT TMPVSKACWL TSDDKKKLDE
FIRLKGLAIA YDKDANPVFL AESDWILRMN MQNNPDIKFH FTSEFKTAVE A
//
