ID A0A372BU62_9GAMM Unreviewed; 533 AA.
AC A0A372BU62;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DZK25_10590 {ECO:0000313|EMBL:RFF26922.1};
OS Wenzhouxiangella sp. 15181.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=2301224 {ECO:0000313|EMBL:RFF26922.1, ECO:0000313|Proteomes:UP000262558};
RN [1] {ECO:0000313|EMBL:RFF26922.1, ECO:0000313|Proteomes:UP000262558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15181 {ECO:0000313|EMBL:RFF26922.1,
RC ECO:0000313|Proteomes:UP000262558};
RA Han S.;
RT "Wenzhouxiangella salilacus sp. nov., a novel bacterium isolated from a
RT saline lake in Xinjiang Province, China.";
RL Submitted (AUG-2018) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFF26922.1}.
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DR EMBL; QUZL01000040; RFF26922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372BU62; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000262558; 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; cd03689; RF3_II; 1.
DR CDD; cd16259; RF3_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:UP000262558}.
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 533 AA; 59970 MW; 339001F87A06C1E3 CRC64;
MPRLTDEIER RRTFAIISHP DAGKTTLTEK FLLFGGAIQL AGSVKSRKAS RHATSDWMEM
EKERGISITS SVMQFPYHER IVNLLDTPGH ADFSEDTYRV LTAVDSALMV IDCAKGVEER
TIKLMDVCRM RDTPIFTFIN KLDREGREPI ELLDEVEEVL GIECAPVTWP IGMGRRLKGI
YHLLRDEIHI YESGKNYMRQ DPQVIAGIDS PEADEALGDM AAELRDEIEL VAGASHDFDL
ARYLKGEQTP VFFGSALNNF GVIPLLDEFV EHAPQPQPRA TLSRDVDPSE EKVTGFVFKV
QANMDPAHRD RMAFMRVCSG RFEKGMKLHH VRIGKEQRTH GALTFMADER ATAEYAYPGD
IVGLHNHGTI GIGDTFTEGE KLQFAGIPSF APELFRRVQL KDPLKLKALT KGLTQLSEEG
ATQFFKPLIG NDLVVGAVGL LQFDVVAYRL KEEYNVEAVF EAVNVATCRW VSADSDRELE
KFRNKNEQHL AEDGGGRLVY LAPTRVNLQL AEERHPEITF RATREVSVYV DTD
//
