RF3_NOSP7
ID RF3_NOSP7 Reviewed; 542 AA.
AC B2J573;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Npun_R3846;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001037; ACC82230.1; -; Genomic_DNA.
DR RefSeq; WP_012410201.1; NC_010628.1.
DR AlphaFoldDB; B2J573; -.
DR SMR; B2J573; -.
DR STRING; 63737.Npun_R3846; -.
DR EnsemblBacteria; ACC82230; ACC82230; Npun_R3846.
DR KEGG; npu:Npun_R3846; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_3; -.
DR OMA; GFVFKIH; -.
DR OrthoDB; 164090at2; -.
DR PhylomeDB; B2J573; -.
DR Proteomes; UP000001191; 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; 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; 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..542
FT /note="Peptide chain release factor 3"
FT /id="PRO_1000092490"
FT DOMAIN 14..283
FT /note="tr-type G"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ SEQUENCE 542 AA; 61388 MW; 43E176C6E7620163 CRC64;
MSTELQSELI QAVELRRNFA IISHPDAGKT TLTEKLLLYG GAIHEAGAVK ARRAQRKATS
DWMAMEQQRG ISITSTVLQF EYQKCQINLL DTPGHQDFSE DTYRTLAAAD NAVMLIDAAK
GLEPQTRKLF EVCKLRGIPI FTFINKLDRP GREPLELLDE IEQELGLQTY AVNWPIGMGD
RFKGVFDRHK QQIHLFERSA HGSREARDTI VELGDPRIEE KLEQSLYYQL KNDLELLEGV
GPELDLQLVH EGKMTPVFFG SAMTNFGVEL FLKYFLEYAL KPGSHYSSVG EVAPTYPEFS
GFVFKLQANM DPKHRDRVAF IRVCTGKFEK DMMVNHARIG KLIRLSRPQK LFAQERESID
VAYPGDVIGL NNPGVFAIGD TIYTGQKLEY EGIPYFSPEL FASLRNPNPS KSKQFQKGVA
ELREEGAVQI MYSTDEAKRD PILAAVGQLQ FEVVQFRLQN EYGVETILDL LPYSVARWVE
GGWEALEKVG RIFNTTTVKD SMGRPVLLFR NEWNCQQLLG DHPELKLSAI APVFSSQQPV
EE