(data stored in ACNUC7421 zone)

HOGENOM: VIBSE_1_PE1015

ID   VIBSE_1_PE1015                       STANDARD;      PRT;   529 AA.
AC   VIBSE_1_PE1015; D0LZV1;
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 1; Short=RF-3 1;
DE   (VIBSE_1.PE1015).
GN   Name=prfC1; OrderedLocusNames=VEA_002625;
OS   VIBRIO SP. EX25.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=150340;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS VIBSE_1.PE1015.
CC       Vibrio sp. Ex25 chromosome chromosome 1, complete sequence.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:D0LZV1_VIBSE
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; D0LZV1; -.
DR   EMBL; CP001805; ACY50787.1; -; Genomic_DNA.
DR   RefSeq; YP_003285252.1; NC_013456.1.
DR   STRING; D0LZV1; -.
DR   GeneID; 8556353; -.
DR   GenomeReviews; CP001805_GR; VEA_002625.
DR   KEGG; vex:VEA_002625; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; VIBSE_1.PE1015; -.
KW   peptide chain release factor 3;
KW   Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   529 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSNTPFLSEV SKRRTFAIIS HPDAGKTTIT EKVLLFGNAI QKAGTVKGRG NAQHAKSDWM
     EMEKERGISV TTSVMQFPYN DCLVNLLDTP GHEDFSEDTY RTLTAVDSCL MVIDAAKGVE
     DRTRKLMEVT RLRDTPIVTF MNKLDRDVRD PMEVLDEVEN ELGMMCAPIT WPIGCGKEFK
     GVYHIHRDET ILYESGHGHE IQEVRIIKGL DNPELDEKVG AGLAESVREE LELVMGACPE
     FDLEMFLTGD LTPVYFGTAL GNFGVDHMLD GLTEWAPAPK TRQAVEREVE ATEEKFSGFV
     FKIQANMDPK HRDRIAFMRI VSGTYTQGMK MNHVRLGKQV SISDAVTFMA GDRSRAEHAY
     AGDIIGLHNH GTIQIGDTFT QGESLKFSGI PNFAPELFRR IRLKDPLKQK QLLKGLVQLS
     EEGAVQVFRP LQNNDLIVGA VGVLQFDVVV ARLKSEYNVE AIYEGINVAT ARWVECDDAK
     KLDEFQRKNQ ANLALDGGDN LTYIAPTMVN LNLAKERFPD IDFRATREH
//

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