(data stored in SCRATCH zone)

SWISSPROT: Q47T20_THEFY

ID   Q47T20_THEFY            Unreviewed;       542 AA.
AC   Q47T20;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 119.
DE   RecName: Full=Peptide chain release factor 3 {ECO:0000256|HAMAP-Rule:MF_00072, ECO:0000256|SAAS:SAAS01159251};
DE            Short=RF-3 {ECO:0000256|HAMAP-Rule:MF_00072};
GN   Name=prfC {ECO:0000256|HAMAP-Rule:MF_00072};
GN   OrderedLocusNames=Tfu_0359 {ECO:0000313|EMBL:AAZ54397.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54397.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Increases the formation of ribosomal termination
CC       complexes and stimulates activities of RF-1 and RF-2. It binds
CC       guanine nucleotides and has strong preference for UGA stop codons.
CC       It may interact directly with the ribosome. The stimulation of RF-
CC       1 and RF-2 is significantly reduced by GTP and GDP, but not by
CC       GMP. {ECO:0000256|HAMAP-Rule:MF_00072,
CC       ECO:0000256|SAAS:SAAS01159261}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00072,
CC       ECO:0000256|SAAS:SAAS01159242}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. PrfC
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00072,
CC       ECO:0000256|SAAS:SAAS01159256}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00072}.
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DR   EMBL; CP000088; AAZ54397.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0359; -.
DR   EnsemblBacteria; AAZ54397; AAZ54397; Tfu_0359.
DR   KEGG; tfu:Tfu_0359; -.
DR   eggNOG; ENOG4105C8A; Bacteria.
DR   eggNOG; COG4108; LUCA.
DR   HOGENOM; HOG000236725; -.
DR   KO; K02837; -.
DR   OMA; VFKIHAN; -.
DR   BioCyc; TFUS269800:G1G4Q-361-MONOMER; -.
DR   Proteomes; UP000000434; 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   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_C_sf.
DR   InterPro; IPR041732; RF3_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_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;
DR   PRODOM; Q47T20.
DR   SWISS-2DPAGE; Q47T20.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS01159255};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS01159253};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS01159239};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS01159247};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN       20    287       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      97    101       GTP. {ECO:0000256|HAMAP-Rule:MF_00072}.
SQ   SEQUENCE   542 AA;  58907 MW;  B21A4F5025AE9B24 CRC64;
     MVSVAAQTST GANEVNREAA RRRTFAVISH PDAGKSTLTE ALALHTEAIT SAGAVHGKGD
     RKGVISDWME IEQDRGISIT SAALRLEYNG CVLNLLDTPG HADFSEDTYR VLSAVDCAVM
     LLDSAKGLEP QTLKLFDVAR SRGIPVITFV NKWDRPGREP LELLDEIEQR IGLRPTPLNW
     PVGVAGDFRG LIDRTAGNRY TKLHRTPGGA TKAREEPMDA VQAAEVEGAA WEQAMEELAL
     LEEIGADYDE ESFLAGKSSP VLFGAALPNF GVSALLRALI NLAPAPAARL DVTGAPRPVD
     APFSGFVFKM QANMDRAHRD RMAFVRVCSG RFDRGMVLTH ATTGRPFATK YAQAVRGAQR
     QTVDTAFPGD VIALVNAQAL RVGDTLYAGP KVEFPPIPSF APEHFAVARA VDSSRYKQFR
     RGIEQLDSEG VVQVLVSDVR GEQAPVLAAV GPLQFDVVTH RMEHEFRAPV ELTHLDYSVA
     RRTDAASAPV LHGLSGAEVL TRRSDGELLV LVHNKWRLKV IQRDHPDLVM EPLLAGGLVE
     EE
//

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