RF3_PSEAE
ID RF3_PSEAE Reviewed; 527 AA.
AC Q9HXB0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=PA3903;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG07290.1; -; Genomic_DNA.
DR PIR; B83159; B83159.
DR RefSeq; NP_252592.1; NC_002516.2.
DR RefSeq; WP_003093004.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXB0; -.
DR SMR; Q9HXB0; -.
DR STRING; 287.DR97_3963; -.
DR PaxDb; Q9HXB0; -.
DR PRIDE; Q9HXB0; -.
DR EnsemblBacteria; AAG07290; AAG07290; PA3903.
DR GeneID; 878928; -.
DR KEGG; pae:PA3903; -.
DR PATRIC; fig|208964.12.peg.4088; -.
DR PseudoCAP; PA3903; -.
DR HOGENOM; CLU_002794_2_1_6; -.
DR InParanoid; Q9HXB0; -.
DR OMA; GFVFKIH; -.
DR PhylomeDB; Q9HXB0; -.
DR BioCyc; PAER208964:G1FZ6-3976-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016150; F:translation release factor activity, codon nonspecific; IBA:GO_Central.
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 GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR CDD; cd04169; RF3; 1.
DR Gene3D; 3.30.70.3280; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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..527
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000210955"
FT DOMAIN 9..277
FT /note="tr-type G"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ SEQUENCE 527 AA; 59865 MW; 9C3C3645F502175C CRC64;
MTTQAAEVAK RRTFAIISHP DAGKTTITEK LLLMGKAIAV AGTVKSRKSD RHATSDWMEM
EKQRGISITT SVMQFPYREH MINLLDTPGH EDFSEDTYRT LTAVDSALMV LDGGKGVEPR
TIALMEVCRL RDTPIVSFIN KLDRDIRDPI ELLDEIEAVL KIKAAPITWP IGCYKDFKGV
YHLADDRIIV YVPGHGHERI ETKVIEKLDS DEARAHLGDL YDNFVEELEL VQGACHEFDK
DAFLKGEMTP VFFGTALGNF GVDQVLDCIV DWAPQPLSRA THERSVEPTE EKFSGFVFKI
QANMDPKHRD RIAFMRICSG KYEKGMKMRH VRLGKDVKIA DALTFFSSER EQLEEAYAGD
IIGLHNHGTI QIGDTFSEGE NFGFTGIPHF APELFRRVRL KDPLKSKQLR QGLQELAEEG
ATQVFFPERN NDIILGAVGV LQFDVVASRL KEEYKVECAY EAINVWSARW IECDDEKKLK
EFKDKAFENL SVDGGGHLTY LAPTRVNLSL MEERWPDIRF RATREHH
