RF3_SYNAS
ID RF3_SYNAS Reviewed; 529 AA.
AC Q2LWC5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SYNAS_25100;
GN ORFNames=SYN_00848;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC78388.1; -; Genomic_DNA.
DR RefSeq; WP_011418408.1; NC_007759.1.
DR AlphaFoldDB; Q2LWC5; -.
DR SMR; Q2LWC5; -.
DR STRING; 56780.SYN_00848; -.
DR EnsemblBacteria; ABC78388; ABC78388; SYN_00848.
DR KEGG; sat:SYN_00848; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_7; -.
DR OMA; GFVFKIH; -.
DR OrthoDB; 164090at2; -.
DR Proteomes; UP000001933; 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; -; 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..529
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000242222"
FT DOMAIN 7..275
FT /note="tr-type G"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 84..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ SEQUENCE 529 AA; 59990 MW; 1C727A3F7CCFCEE7 CRC64;
MYQKEIEQRR TFGIISHPDA GKTTLTEKLL LFGGAIQLAG TVKARKATRH ATSDWMAIEK
ERGISVTTSV MKFHYRDFEI NLLDTPGHQD FSEDTYRVLT AVDSAVMVID GAKGVEPQTE
KLMEICLLRN TPVITFINKL DREVLSPLEL LADIEKKLQI ECVPMSWPIG MGKSFRGVYN
LYRRELQLFT PGASTRGGEV FVIRDLDDPE LDRRLGSQAD ELREDIALME GAANPFVYEH
FLKANQTPVF FGSAINNFGV RELLDAVVEL APSPRPRLAT TREVLPSEEQ FSGFAFKIQA
NMDSAHRDRI AFVRICSGKF TRGMKVRHNR IGKDVTLANA TIFMAQDRAS VEEAYPGDII
GIHNHGTIRI GDTFTEGEEL RFTGIPNFAP EHFCRVRLKN PLKTKQLQKG LNQLSEEGIV
QVFRPLTSND YILGVVGVLQ FDVTMVRLLN EYGVEADYES VDYAAARWVT CPEREKLENF
EKQHRSNLAL DSEGNLIYLA LSQWRLSNTM EEWPDITMHK TMEHSQRLN
