RF3_SALTY
ID RF3_SALTY Reviewed; 529 AA.
AC Q56121;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Peptide chain release factor 3;
DE Short=RF-3;
GN Name=prfC; OrderedLocusNames=STM4560;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7559341; DOI=10.1128/jb.177.19.5547-5553.1995;
RA Kawazu Y., Ito K., Matsumura K., Nakamura Y.;
RT "Comparative characterization of release factor RF-3 genes of Escherichia
RT coli, Salmonella typhimurium, and Dichelobacter nodosus.";
RL J. Bacteriol. 177:5547-5553(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC {ECO:0000305}.
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DR EMBL; D50496; BAA09090.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23375.1; -; Genomic_DNA.
DR RefSeq; NP_463416.1; NC_003197.2.
DR RefSeq; WP_000175965.1; NC_003197.2.
DR AlphaFoldDB; Q56121; -.
DR SMR; Q56121; -.
DR STRING; 99287.STM4560; -.
DR PaxDb; Q56121; -.
DR PRIDE; Q56121; -.
DR EnsemblBacteria; AAL23375; AAL23375; STM4560.
DR GeneID; 1256086; -.
DR KEGG; stm:STM4560; -.
DR PATRIC; fig|99287.12.peg.4801; -.
DR HOGENOM; CLU_002794_2_1_6; -.
DR OMA; GFVFKIH; -.
DR PhylomeDB; Q56121; -.
DR BioCyc; SENT99287:STM4560-MON; -.
DR Proteomes; UP000001014; 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; -; 3.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..529
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000210960"
FT DOMAIN 11..280
FT /note="tr-type G"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 165
FT /note="G -> A (in Ref. 1; BAA09090)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="A -> P (in Ref. 1; BAA09090)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="V -> E (in Ref. 1; BAA09090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 59563 MW; 88FCE03468648834 CRC64;
MTLSPYLQEV AKRRTFAIIS HPDAGKTTIT EKVLLFGQAI QTAGTVKGRG SSQHAKSDWM
EMEKQRGISI TTSVMQFPYH DCLVNLLDTP GHEDFSEDTY RTLTAVDCCL MVIDAAKGVE
DRTRKLMEVT RLRDTPILTF MNKLDRDIRD PMELLDEVEN ELKIGCAPIT WPIGCGKLFK
GVYHLYKDET YLYQTGKGHT IQEVRIVKGL NNPDLDAAVG EDLAQQLRDE LELVQGASNE
FDEELFLAGE ITPVFFGTAL GNFGVDHMLD GLVAWAPAPM PRQTDTRTVE ASEEKFTGFV
FKIQANMDPK HRDRVAFMRV VSGKYEKGMK LRQVRTGKDV VISDALTFMA GDRSHVEEAY
PGDILGLHNH GTIQIGDTFT QGEMMKFTGI PNFAPELFRR IRLKDPLKQK QLLKGLVQLS
EEGAVQVFRP ISNNDLIVGA VGVLQFDVVV ARLKSEYNVE AIYESVNVAT ARWVESADAK
KFEEFKRKNE TQLALDGGDN LTYIAPTMVN LNLTQERYPD VQFRKTREH
