RF3_LISMO
ID RF3_LISMO Reviewed; 522 AA.
AC Q8Y8C0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=lmo0988;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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 {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; AL591977; CAC99066.1; -; Genomic_DNA.
DR PIR; AD1198; AD1198.
DR RefSeq; NP_464513.1; NC_003210.1.
DR RefSeq; WP_003722853.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y8C0; -.
DR SMR; Q8Y8C0; -.
DR STRING; 169963.lmo0988; -.
DR PaxDb; Q8Y8C0; -.
DR EnsemblBacteria; CAC99066; CAC99066; CAC99066.
DR GeneID; 986429; -.
DR KEGG; lmo:lmo0988; -.
DR PATRIC; fig|169963.11.peg.1016; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_9; -.
DR OMA; GFVFKIH; -.
DR PhylomeDB; Q8Y8C0; -.
DR BioCyc; LMON169963:LMO0988-MON; -.
DR Proteomes; UP000000817; 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; -; 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..522
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000210949"
FT DOMAIN 10..277
FT /note="tr-type G"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 87..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ SEQUENCE 522 AA; 59400 MW; 5EB688A5A15BC5E3 CRC64;
MSQDLQKEVA SRKTFAIISH PDAGKTTITE QLLLFGGVIR SAGTVKGKKS GKFATSDWME
IEKQRGISVT SSVMQFDYNG SRINILDTPG HSDFSEDTYR TLMAVDSAVM VIDAAKGIEA
QTLKLFKVCR MRGIPIFTFI NKMDRQGKMP LELLAELEEV LGIESYPMNW PIGMGKELAG
LYDRYHRVIE QYRSEEDERF LPLGEDGDLK EAHAIQKSLY YDQALEEIML LDEAGNDFSR
ERIIAGEQTP VFFGSALTNF GVETFLRTFV DFAPAPSSHE SNEGVIEADN PKFSGFIFKI
QANMNPAHRD RIAFIRICSG EFERGMNVTL TRTGKSLKLA NSTQFMADDR ETVNRAVAGD
IIGLYDTGNY QIGDTITNGS KKLEFEKLPQ FTPELFMRVY AKNVMKQKHF HKGVEQLVQE
GAIQLFKTWR TEEYIIGAVG QLQFEVFEHR MRGEYNSEIR MEPIGKKIAR WVKEEDADEK
LSTARSMLVK DRFDQPLFLF ENEFAINWFN DKNPDIELTS LL
