ID A0A2U8E4Q5_9BACT Unreviewed; 548 AA.
AC A0A2U8E4Q5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-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 ORFNames=CKA38_11815 {ECO:0000313|EMBL:AWI09843.1};
OS Ereboglobus luteus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Ereboglobus.
OX NCBI_TaxID=1796921 {ECO:0000313|EMBL:AWI09843.1, ECO:0000313|Proteomes:UP000244896};
RN [1] {ECO:0000313|EMBL:AWI09843.1, ECO:0000313|Proteomes:UP000244896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ho45 {ECO:0000313|EMBL:AWI09843.1,
RC ECO:0000313|Proteomes:UP000244896};
RX PubMed=29295750; DOI=10.1016/j.syapm.2017.10.005;
RA Tegtmeier D., Belitz A., Radek R., Heimerl T., Brune A.;
RT "Ereboglobus luteus gen. nov. sp. nov. from cockroach guts, and new
RT insights into the oxygen relationship of the genera Opitutus and
RT Didymococcus (Verrucomicrobia: Opitutaceae).";
RL Syst. Appl. Microbiol. 41:101-112(2018).
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; CP023004; AWI09843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8E4Q5; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000244896; 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; 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:UP000244896}.
FT DOMAIN 8..277
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 548 AA; 60547 MW; 8F6C14C7659380FA CRC64;
MSPAAEIARR RTFAIISHPD AGKTTLTEKF LLYGNAIHLA GTVTARKNQR ATTSDWMELE
KQRGISVSST VLQFDYNGCA VNLLDTPGHK DFSEDTYRVL TAVDAALMVI DAGKGVEPQT
RKLFEVCRRR GIPIFTFMNK CDRPTLDPLA LIDELESVLG IAASPIVWPL GSGPSFRGVF
DRTERAVHLF ERVPNGAYEA PVNITGLDDP AVRGKLDDHT FNESTEQLAM LDGAGHPLDL
AAIHAGQQTP VYFGSAINNF GIQLLLDGFL KHSVPPAPRR SVSITVPGAP APTEAREVPV
DYEKFSGFIF KIQANMDPKH RDRIAFLRVC SGRFTRDMVV AHQRTGKQVR LSSSHKLFGQ
ERETVNEAWP GDVIGLVGHD AFGIGDTLTE DRAIAYDEIP RFPPEVFAYL SNPTSSDAKK
YRAGLEQLLQ EGVVQSFTPR NAPPGATLLA AVGPLQFEVV QWRLKSEYNA ESRLEQTNWT
LLKWLEPHPS LANPSALVVA SGVSFGTDKF DNPVALFPND WTMRYFMEKN PDLKLHDMPI
EQIKAAAE
//
