RF3_AROAE
ID RF3_AROAE Reviewed; 548 AA.
AC Q5P409;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Peptide chain release factor 3 {ECO:0000255|HAMAP-Rule:MF_00072};
DE Short=RF-3 {ECO:0000255|HAMAP-Rule:MF_00072};
GN Name=prfC {ECO:0000255|HAMAP-Rule:MF_00072}; OrderedLocusNames=AZOSEA18290;
GN ORFNames=ebA3251;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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:0000255|HAMAP-Rule:MF_00072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00072}.
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DR EMBL; CR555306; CAI07954.1; -; Genomic_DNA.
DR RefSeq; WP_011237663.1; NC_006513.1.
DR AlphaFoldDB; Q5P409; -.
DR SMR; Q5P409; -.
DR STRING; 76114.ebA3251; -.
DR EnsemblBacteria; CAI07954; CAI07954; ebA3251.
DR KEGG; eba:ebA3251; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_4; -.
DR OMA; TPASWPI; -.
DR OrthoDB; 164090at2; -.
DR Proteomes; UP000006552; 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; 3.30.70.3280; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43556; PTHR43556; 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 1.
DR TIGRFAMs; TIGR00503; prfC; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..548
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000242169"
FT DOMAIN 23..290
FT /note="tr-type G"
FT BINDING 32..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 100..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 154..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ SEQUENCE 548 AA; 61117 MW; 4D5E0C59FC96D12A CRC64;
MADIPAATPS ATPFPPELLR DVERRRTFGI ISHPDAGKTT LTEKLLLFGG AIQLAGTVKA
RKSARHATSD WMEVEKQRGI SVSSSVMQFE YAGHTINLLD TPGHQDFSED TYRVLTAVDA
AVMVIDAAKG VETQTIKLLE VCRLRNTPII TFINKMDREV RESFDLLQEI EEVLKIDCAP
ITWPIGMGKT FRGVYHLLED RVLRFTPGEE KRSEAEVIKG IANAQLDELF PLEVGKLREE
VDLIQGASNP FSLGDFLAGK QTPVFFGSGI NNFGVQEILQ ALLDWAPPPQ PRVAGVTVAD
TRLVMPAEAP FSGFVFKIQA NMDPKHRDRI AFFRICSGRY SSGMKVKHVR MGREMKLANA
LTFMANERVL MEDGVAGDII GIHNHGQLHI GDTLTEGENL GYKGIPYFSP ELFSAARLRD
PLKSKQLQKG LQELGEEGAI QVFEQEGGNM LLGAVGQLQF EVVAQRLKDE YKVDAIFESA
DIYTARWLVF PDEVTRRNFE REQGIRVGKD VDGNPVYLAT SRYNLEVTME KWPKVGFHAT
REHGEKLS
