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Database: UniProt
Entry: A0A1W6CXU5_9RHOB
LinkDB: A0A1W6CXU5_9RHOB
Original site: A0A1W6CXU5_9RHOB 
ID   A0A1W6CXU5_9RHOB        Unreviewed;       532 AA.
AC   A0A1W6CXU5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Peptide chain release factor 3 {ECO:0000256|HAMAP-Rule:MF_00072};
DE            Short=RF-3 {ECO:0000256|HAMAP-Rule:MF_00072};
GN   Name=prfC {ECO:0000256|HAMAP-Rule:MF_00072};
GN   ORFNames=B0A89_08575 {ECO:0000313|EMBL:ARJ69665.1};
OS   Paracoccus contaminans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ69665.1, ECO:0000313|Proteomes:UP000193017};
RN   [1] {ECO:0000313|EMBL:ARJ69665.1, ECO:0000313|Proteomes:UP000193017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC   {ECO:0000313|Proteomes:UP000193017};
RA   Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT   "Genome sequence of Paracoccus contaminans isolated from a water
RT   microcosm.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Increases the formation of ribosomal termination complexes
CC       and stimulates activities of RF-1 and RF-2. It binds guanine
CC       nucleotides and has strong preference for UGA stop codons. It may
CC       interact directly with the ribosome. The stimulation of RF-1 and RF-2
CC       is significantly reduced by GTP and GDP, but not by GMP.
CC       {ECO:0000256|HAMAP-Rule:MF_00072}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00072}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC       {ECO:0000256|ARBA:ARBA00009978, ECO:0000256|HAMAP-Rule:MF_00072}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00072}.
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DR   EMBL; CP020612; ARJ69665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6CXU5; -.
DR   STRING; 1945662.B0A89_08575; -.
DR   KEGG; pcon:B0A89_08575; -.
DR   OrthoDB; 9802948at2; -.
DR   Proteomes; UP000193017; 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   CDD; cd16259; RF3_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 1.
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; IPR038467; RF3_dom_3_sf.
DR   InterPro; IPR041732; RF3_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00503; prfC; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43556; PEPTIDE CHAIN RELEASE FACTOR RF3; 1.
DR   PANTHER; PTHR43556:SF2; PEPTIDE CHAIN RELEASE FACTOR RF3; 1.
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; SSF54980; EF-G C-terminal domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00072};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00072};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00072}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193017}.
FT   DOMAIN          13..282
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         90..94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   532 AA;  59389 MW;  A6835F58E07AA8A2 CRC64;
     MLDNRPQLPP EIARRRTFAI IAHPDAGKTT LTEKFLLFGG AIQMAGQVRA KGEARRTRSD
     FMKMEQDRGI SVSASAMSFD FGPYRFNLVD TPGHSDFSED TYRTLTAVDA AIMVIDGAKG
     VESQTRKLFE VCRLRDLPIL TFCNKMDREA RDTFEIIDEI QENLAIDVVP ASWPIGSGRD
     FIGTYDLLND RLELMDRADR NRVAESVKIE GLDDPALGRH IPADALAKLR DEIEMARELL
     PAFDRKSFLE GHMTPIWFGS AINSFGVKEL MQGIGEYGPQ PQPQSAAERQ IAPEEDRVAG
     FVFKVQANMD PKHRDRVAFV RLASGHFERG MKLLHVRSKK PMAVSNPVLF LAADRELAEE
     AWAGDIIGIP NHGQLRIGDA LTEGEALRFT GIPSFAPELL QTVRAGDPMK AKHLEKALMQ
     FAEEGAAKVF RPMIGSGFIV GVVGALQFDV LASRIEQEYG LPVRFEPSQF TSARWLSGPK
     DAVEKFAATN KQHMASDNDG DLVYLTRLQW DIDRVQRDQP ELKLTATKEM MV
//
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