(data stored in ACNUC7421 zone)

HOGENOM: RALPJ_1_PE1

ID   RALPJ_1_PE1                          STANDARD;      PRT;   531 AA.
AC   RALPJ_1_PE1; B2UH26;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Peptide chain release factor 3; (RALPJ_1.PE1).
GN   OrderedLocusNames=Rpic_3761;
OS   RALSTONIA PICKETTII 12J.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RALPJ_1.PE1.
CC       Ralstonia pickettii 12J chromosome 2, complete sequence.
CC       96802056..97720880 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:B2UH26_RALPJ
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 GMP
CC       (By similarity).
CC   -!- GENE_FAMILY: HOG000236725 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B2UH26; -.
DR   EMBL; CP001069; ACD28877.1; -; Genomic_DNA.
DR   RefSeq; YP_001892304.1; NC_010678.1.
DR   STRING; B2UH26; -.
DR   GeneID; 6284993; -.
DR   GenomeReviews; CP001069_GR; Rpic_3761.
DR   KEGG; rpi:Rpic_3761; -.
DR   OMA; LQFEVVQ; -.
DR   ProtClustDB; PRK00741; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:HAMAP.
DR   GO; GO:0006449; P:regulation of translational termination; IEA:HAMAP.
DR   HAMAP; MF_00072; Rel_fac_3; 1; -.
DR   InterPro; IPR009022; Elongation_fac_G/III/V.
DR   InterPro; IPR004548; PrfC.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF54980; EFG_III_V; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00503; PrfC; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; 1.
DR   HOGENOMDNA; RALPJ_1.PE1; -.
KW   peptide chain release factor 3;
KW   Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   531 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTLQQEIRR RRTFAIIAHP DAGKTTLTEK LLWFGGAIQM AGAVRARKAN RHATSDWMEM
     EKQRGISVTS SVMQFPYRNE GGDYIVNLLD TPGHEDFSED TYRTLTAVDS AVMVIDSVNG
     VEAQTIKLLN VCRLRSTPIL TFINKLDREG RAPIELLDEI ESVLQIQCAP MTWPIGMGKS
     FKGVYHLVND TVQLFDPNAD SEKGATAGLI QGLDNPELDR VLGSQAEELR IDIELVRGAS
     HTFDKEAFLA GKQCPVYFGS AVNNFGVQSL LDALVDQSPE PLARPTETRE VKPMEEKFTG
     FVFKIQANMD PKHRDRIAFV RVCSGRFERG MKLLQVSTGK TVAINNAITF MAQDRNTTEE
     AFAGDIIGVP NHGTIRLGDA FTEGEALKFT GIPSFAPEFF RRARLNNPLR LKQLQKGLQQ
     LAEEGATQMF RPLASNDLVL GAVGILQFDV VAHRLEHEYG VDAIFEPHEC STARWLRGKQ
     EDIDKLIDKA GHNVALDGAG DYVYLAPSQV NLRLTQERFP DIQFMETREI V
//

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