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Database: UniProt
Entry: A0A167IBH2_9BURK
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ID   A0A167IBH2_9BURK        Unreviewed;       539 AA.
AC   A0A167IBH2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ECO:0000313|EMBL:OAD42465.1};
GN   ORFNames=LPB072_05640 {ECO:0000313|EMBL:AOW12414.1}, LPB72_08220
GN   {ECO:0000313|EMBL:OAD42465.1};
OS   Hydrogenophaga crassostreae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1763535 {ECO:0000313|EMBL:AOW12414.1, ECO:0000313|Proteomes:UP000185680};
RN   [1] {ECO:0000313|EMBL:OAD42465.1, ECO:0000313|Proteomes:UP000185657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0072 {ECO:0000313|EMBL:OAD42465.1,
RC   ECO:0000313|Proteomes:UP000185657};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Hydrogenophaga sp. LPB0072.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOW12414.1, ECO:0000313|Proteomes:UP000185680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0072 {ECO:0000313|EMBL:AOW12414.1,
RC   ECO:0000313|Proteomes:UP000185680};
RA   Kim E., Yi H.;
RT   "Hydorgenophaga sp. LPB0072 isolated from gastropod.";
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}.
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DR   EMBL; CP017476; AOW12414.1; -; Genomic_DNA.
DR   EMBL; LVWD01000008; OAD42465.1; -; Genomic_DNA.
DR   RefSeq; WP_066088626.1; NZ_LVWD01000008.1.
DR   AlphaFoldDB; A0A167IBH2; -.
DR   STRING; 1763535.LPB072_05640; -.
DR   KEGG; hyl:LPB072_05640; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000185657; Unassembled WGS sequence.
DR   Proteomes; UP000185680; 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: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   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:UP000185680}.
FT   DOMAIN          9..277
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   539 AA;  59666 MW;  0BA83372E11E46DD CRC64;
     MSEIAKQVRR RRTFAIISHP DAGKTTLTEK LLLFSGAINI AGSVKARKAA RHATSDWMEI
     EKQRGISVAS SVMQMEYRDC VINLLDTPGH QDFSEDTYRV LTAVDAALMV IDAGNGVEPQ
     TRRLLQVCRA RNTPILTFVN KMDREVQSPL DLMDEIEREL GMTVVPFTWP VGMGKTFRGV
     FDRRTDQMRV FSAGEDRRGG EEEALIGLDN PESVKRFGSD FEQAKEELEL VAGASTAFDK
     EEFLAGRQTP MLFGSAVNNF GVREVLDALV DLAPPPGDRP AMQRVVKPEE PKFTGVVFKI
     QANMDPAHRD RIAFVRLASG HFQRGMKIKV VRSGKDLRPN TVVSFLSQRR ELLDEAFAGD
     IIGIPNHGVL QLGDTLTEGE NLQFTGLPFF APEIIRSVEV ADPLRTKQLR AGLTQLGEEG
     AIQVFRPVAG SVLLLGAVGQ LQFEVVAHRL EHEYGVKARI MGSPYQVARW VTCAPEDGGE
     IELKKFIDAN SHRVALDAVD APTLLVDHAA TLRAVEANWP KIKFHAMREH AGLVFHTGV
//
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