(data stored in ACNUC7421 zone)

HOGENOM: SHEDO_1_PE1012

ID   SHEDO_1_PE1012                       STANDARD;      PRT;   527 AA.
AC   SHEDO_1_PE1012; Q12QG7;
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   RecName: Full=Peptide chain release factor 3; Short=RF-3;
DE   (SHEDO_1.PE1012).
GN   Name=prfC; OrderedLocusNames=Sden_1021;
OS   SHEWANELLA DENITRIFICANS OS217.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHEDO_1.PE1012.
CC       Shewanella denitrificans OS217, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:RF3_SHEDO
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       PrfC subfamily.
CC   -!- GENE_FAMILY: HOG000236725 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q12QG7; -.
DR   EMBL; CP000302; ABE54309.1; -; Genomic_DNA.
DR   RefSeq; YP_562032.1; NC_007954.1.
DR   ProteinModelPortal; Q12QG7; -.
DR   SMR; Q12QG7; 7-527.
DR   STRING; Q12QG7; -.
DR   GeneID; 4016589; -.
DR   GenomeReviews; CP000302_GR; Sden_1021.
DR   KEGG; sdn:Sden_1021; -.
DR   NMPDR; fig|318161.14.peg.1002; -.
DR   eggNOG; COG4108; -.
DR   OMA; HERTVEP; -.
DR   PhylomeDB; Q12QG7; -.
DR   ProtClustDB; PRK00741; -.
DR   BioCyc; SDEN318161:SDEN_1021-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:InterPro.
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; SHEDO_1.PE1012; -.
KW   peptide chain release factor 3;
KW   Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   527 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLGNHAEVDI RRTFAIISHP DAGKTTITEK VLLFGQAIQV AGTVKGRGSK QHAKSDWMEM
     EKDRGISITT SVMQFPYKDC LVNLLDTPGH EDFSEDTYRT LTAVDSCLMV IDAAKGVEDR
     TRKLMEVTRL RDTPIITFMN KCDRDIRDPM EVMDEVENEL KIACAPITWP IGCGKSFKGV
     YHLHRDETIL YQSGLGHMMQ EVRIVKGLDN PELDKAIGSE LAEQLREELE LVIGASHEFE
     LAAFLKGELT PVYFGTALGN FGVDHMLDGL TQWAPKPQPR QTEVREVTSL DSDFSGFIFK
     IQANMDPKHR DRVAFMRVVS GKYEKGMKMH HVRVGKDVRI SDALTFVAGD REQVEEAYPG
     DIIGLHNHGT IQIGDTFTQG EKLKFTGIPN FAPEMFRRIR LKDPLKQKQL LKGLVQLAEE
     GAVQVFRPLD NNDLIVGAVG VLQFEVVVGR LKSEYNVEAI YEAINVSTAR WVYCKDERKL
     EEFRRKCSVN LALDGGNNLT YIAPTMVNLN LSMERYPDVA FAKTREN
//

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