ID A0A178IEE9_9BACT Unreviewed; 596 AA.
AC A0A178IEE9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AW736_19540 {ECO:0000313|EMBL:OAM88393.1};
OS Opitutaceae bacterium TSB47.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=1184151 {ECO:0000313|EMBL:OAM88393.1, ECO:0000313|Proteomes:UP000078486};
RN [1] {ECO:0000313|EMBL:OAM88393.1, ECO:0000313|Proteomes:UP000078486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSB47 {ECO:0000313|EMBL:OAM88393.1,
RC ECO:0000313|Proteomes:UP000078486};
RA Wang Y., Shi Y., Qiu Z., Liu S., Yang H.;
RT "High potential of lignocellulose degradation of a new Verrucomicrobia
RT species.";
RL Submitted (JAN-2016) 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}.
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:OAM88393.1}.
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DR EMBL; LRRQ01000137; OAM88393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178IEE9; -.
DR STRING; 1184151.AW736_19540; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000078486; 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; 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; 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:UP000078486}.
FT DOMAIN 8..277
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 277..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 596 AA; 65042 MW; F466010EE961E47A CRC64;
MSPAAEIARR RTFAIISHPD AGKTTLTEKF LLYGNAIHLA GTVTARKNQR ATTSDWMELE
KQRGISVSST VLQFDYAGCA VNLLDTPGHK DFSEDTYRVL TAVDAALMVI DAGRGVQPQT
RKLFEVCRRR GIPIFTFMNK CDRPTLNALA LIDELESVLG LAAAPVIWPL GNGPTFRGVF
DRRARAVHLF ERVPGGAYEA PVNITDLNAP IVRDRLDDYT FNEVTEQLEM LDGAGHPLDL
AAVHAGQQTP VYFGSAINNF GIQLLLDGFL SDSVPPQPRR NASAAAKYQV TSNTSNKNLD
TADAASSRAS GPVATGGGEA ADSLDTCHLP LATSSSAPLA TSPSALVPLE YPKFSGFIFK
IQANMDPKHR DRIAFLRVCS GKFTRDMVVT HQRTGKNVRL SSSHKLFGQE RETVDEAWPG
DVIGLVGHDA FGIGDTLTED RGIAYDEIPR FPPEVFAYLS NPASSDAKKY RAGLEQLLQE
GVVQSFNVRH APPGATLLAA VGPLQFEVVQ WRLKSEYNAE SRLESAPWTL LKWLEPHPAL
ANPSAIIVAS GVSFGTDKFG HPVVLFPNEW TMAYFKEKNP ELIPHDLPLE QVQTAK
//
