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Database: UniProt
Entry: A0A1H8GU53_9RHOB
LinkDB: A0A1H8GU53_9RHOB
Original site: A0A1H8GU53_9RHOB 
ID   A0A1H8GU53_9RHOB        Unreviewed;       532 AA.
AC   A0A1H8GU53;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN04488103_105166 {ECO:0000313|EMBL:SEN47405.1};
OS   Gemmobacter aquatilis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=933059 {ECO:0000313|EMBL:SEN47405.1, ECO:0000313|Proteomes:UP000198761};
RN   [1] {ECO:0000313|EMBL:SEN47405.1, ECO:0000313|Proteomes:UP000198761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3857 {ECO:0000313|EMBL:SEN47405.1,
RC   ECO:0000313|Proteomes:UP000198761};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOCE01000005; SEN47405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8GU53; -.
DR   STRING; 933059.SAMN04488103_105166; -.
DR   OrthoDB; 9802948at2; -.
DR   Proteomes; UP000198761; Unassembled WGS sequence.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 1.
DR   Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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:UP000198761}.
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;  59575 MW;  D33A708AD7BB79AB CRC64;
     MLDNRPTLPP EIARRRTFAI IAHPDAGKTT LTEKFLLFGG AIQMAGQVRA KGEARRTRSD
     FIKMEQERGI SVSASAMSFD FRDYRFNLVD TPGHSDFSED TYRTLTAVDA AVMVIDGAKG
     VESQTRKLFE VCRLRDLPIL TFCNKMDREA RDTFEIIDEI QENLAIDVSP ASWPIGQGRD
     FLGCYDILND RLELMDRADR NRVAETIQIN GLDDPQLADH VPADLLEKLR EELEMARELL
     PVFDRQSFLE GHMTPIWFGS AINSFGVKEL MDGIGKYGPE PQPQPTATRK VAPEESAVTG
     VVFKVQANMD PKHRDRVAFV RLASGHFERG MKLTHVRTKK PMAVANPVMF LAADRELAEE
     AWAGDIIGIP NHGQLRIGDA LTEGEALRFT GIPSFAPELL QGVRAGDPMK AKHLEKALMQ
     FAEEGAAKVF KPMIGSGFIV GVVGALQFEV LASRIEQEYS LPVRFEPSQF TSARWLTGAK
     ADVEKFVNVN KGHIAYDNDG DLVYLTRLRW DIDRVERDHP ELKLTATKEM MV
//
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