(data stored in SCRATCH zone)

SWISSPROT: Q13SB2_PARXL

ID   Q13SB2_PARXL            Unreviewed;       533 AA.
AC   Q13SB2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   30-AUG-2017, entry version 90.
DE   RecName: Full=Peptide chain release factor 3 {ECO:0000256|HAMAP-Rule:MF_00072, ECO:0000256|SAAS:SAAS00669814};
DE            Short=RF-3 {ECO:0000256|HAMAP-Rule:MF_00072};
GN   Name=prfC {ECO:0000256|HAMAP-Rule:MF_00072};
GN   ORFNames=Bxe_B2968 {ECO:0000313|EMBL:ABE33027.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33027.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33027.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33027.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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:SAAS00089113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00072,
CC       ECO:0000256|SAAS:SAAS00336660}.
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:SAAS00534159}.
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DR   EMBL; CP000271; ABE33027.1; -; Genomic_DNA.
DR   RefSeq; WP_011490416.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13SB2; -.
DR   STRING; 266265.Bxe_B2968; -.
DR   EnsemblBacteria; ABE33027; ABE33027; Bxe_B2968.
DR   GeneID; 4006881; -.
DR   KEGG; bxb:DR64_5299; -.
DR   KEGG; bxe:Bxe_B2968; -.
DR   PATRIC; fig|266265.5.peg.4719; -.
DR   eggNOG; ENOG4105C8A; Bacteria.
DR   eggNOG; COG4108; LUCA.
DR   HOGENOM; HOG000236725; -.
DR   KO; K02837; -.
DR   OMA; VFKIHAN; -.
DR   OrthoDB; POG091H00HD; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-HAMAP.
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; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
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;
DR   PRODOM; Q13SB2.
DR   SWISS-2DPAGE; Q13SB2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00089100};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00089095};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00089120};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00414956};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        7    275       Tr-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      16     23       GTP. {ECO:0000256|HAMAP-Rule:MF_00072}.
FT   NP_BIND      84     88       GTP. {ECO:0000256|HAMAP-Rule:MF_00072}.
FT   NP_BIND     138    141       GTP. {ECO:0000256|HAMAP-Rule:MF_00072}.
SQ   SEQUENCE   533 AA;  59281 MW;  9CA60B7DCFC1B678 CRC64;
     MSVSELKRRR TFAVISHPDA GKTTLTEKLL LFSGAIQIAG TVKGRKSNRY ATSDWMEIEK
     QRGISVASSV MQFEYGDAVI NLLDTPGHED FSEDTYRVLT AVDAAVMVID GANGVEAQTL
     KLLEVCRSRK TPIVTFINKL DREVREPLEL LDEIEQHLGV AAVPFTWPIG MGKDFQGVYD
     IQRDQVRLFR AGQDKAGGEV ETLQALSDEE GERRFGHAWV KAKEEIDLIT GASPDFDREQ
     FLAGQQSPVL FGSAINNFGV KEILDALVDL APPPSMRMTV QRPVMPDEPK FTGVVFKVQA
     NMDLAHRDRV AFIRVCSGHF ERGMAVKVTR TSKTFRANNV VTFLSQRRET VSEAYPGDII
     GIPNHGTLSL GDTLTEGEQL QFVGLPFFAP EIFQTVEVVD PMRAKQLGEA LKQLGEEGAI
     QVFRPEVGGL MILGAVGQLQ FEVVSHRLST EYKVDVRMAP ARYRMSRWVT CDDAAELRRF
     TDSYAARIAL DASDAPTYLA SHVSEIEVAQ KAWPKIVFNE LREHSGAPFK RAM
//

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