RF3_TRIEI
ID RF3_TRIEI Reviewed; 542 AA.
AC Q110K2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Tery_2904;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) 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; CP000393; ABG52072.1; -; Genomic_DNA.
DR RefSeq; WP_011612431.1; NC_008312.1.
DR AlphaFoldDB; Q110K2; -.
DR SMR; Q110K2; -.
DR STRING; 203124.Tery_2904; -.
DR PRIDE; Q110K2; -.
DR EnsemblBacteria; ABG52072; ABG52072; Tery_2904.
DR KEGG; ter:Tery_2904; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_3; -.
DR OMA; GFVFKIH; -.
DR OrthoDB; 164090at2; -.
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.
FT CHAIN 1..542
FT /note="Peptide chain release factor 3"
FT /id="PRO_1000023694"
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; 61416 MW; CBA2508EBD472C88 CRC64;
MSIEIEAELQ TAVDKRRNFA IISHPDAGKT TLTEKLLLYG GAIQEAGAVK AKRAQRHATS
DWMAMEQQRG ISITSTVLQF DYQNCQINLL DTPGHQDFSE DTYRTLAAAD NAVMLEDSAK
GLEPQTRKLF EVCKMRKLPI FTFINKMDRP GREPLELLDE IEQELGLKTY PVNWPIGMGD
RFKGVFDRRK EQIHLFERSI HGRKAAVNTV VNLGDPQIEK LLDQDLYYQL KEDLELLDEL
GSALDLEQIH TGEMTPVFFG SAMTNFGVQL FLDAFLEYAL KPGIHKSTVG EVSPTYPNFT
GFVFKLQANM DPKHRDRVAF IRVCTGKFEK DMTVSHARTG KTVRLSRPQK LFAQDRASIE
NAYPGDIIGL NNPGVFAIGD TIYNGKKIEY EGIPCFSPEI FAYLRNPNPS KFKQFRKGVN
ELREEGAVQI MYSADEAKRD PILAAVGQLQ LEVVQFRMQN EYGVETRVEM LPFTVARWVD
GGWEILQKVG RLFNTVAVKD SWGRPVLLFK NQWNCQQVES EHPELKLNNT APVVSGQEPE
SL