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Database: UniProt
Entry: A0A2R8BS08_9RHOB
LinkDB: A0A2R8BS08_9RHOB
Original site: A0A2R8BS08_9RHOB 
ID   A0A2R8BS08_9RHOB        Unreviewed;       535 AA.
AC   A0A2R8BS08;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-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   ECO:0000313|EMBL:SPJ22876.1};
GN   ORFNames=PAA8504_00675 {ECO:0000313|EMBL:SPJ22876.1};
OS   Palleronia abyssalis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Palleronia.
OX   NCBI_TaxID=1501240 {ECO:0000313|EMBL:SPJ22876.1, ECO:0000313|Proteomes:UP000244912};
RN   [1] {ECO:0000313|EMBL:SPJ22876.1, ECO:0000313|Proteomes:UP000244912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8504 {ECO:0000313|EMBL:SPJ22876.1,
RC   ECO:0000313|Proteomes:UP000244912};
RA   Keele B.F.;
RL   Submitted (MAR-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}.
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DR   EMBL; ONZF01000001; SPJ22876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8BS08; -.
DR   OrthoDB; 9802948at2; -.
DR   Proteomes; UP000244912; 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:UP000244912}.
FT   DOMAIN          16..285
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         25..32
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         93..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         147..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   535 AA;  59859 MW;  4A4A9D747DFC4B42 CRC64;
     MLDRSHNAAP LPPEIARRRT FAIISHPDAG KTTLTEKFLL FGGAIQMAGQ VRAKGEARRT
     RSDFMQMEKD RGISVSASAM SFDFGDYRFN LVDTPGHSDF SEDTYRTLTA VDAAVMVIDG
     AKGVESQTQK LFEVCRLRDL PILTFCNKMD RESRDVFEII DEIQENLAID VTPASWPIGV
     GRDFLGCYDM LNDRLELLDR ADRNRVAESI RLNGLDDPKM EEHIPAHMLE KLREEVEMAR
     ELMPAFDAQS LLDGTLTPIW FGSAINSFGV KELMEGIGRF GPQPQPQKAS PRQIAPDENK
     VSGFVFKVQA NMDPKHRDRV AFVRLASGHF KRGMKLTHVR TKKPMAVSNP VLFLASDREL
     AEEAWAGDIM GIPNHGQLRI GDTLTEGEAL RVQGIPSFAP ELLQNCRAGD PMKAKHLDKA
     LMQFAEEGAA KVFKPMLGAG FIVGVVGALQ FEVLASRIEM EYGLPVRFEP SQFSSARWVH
     GPKDKVEAFA QANKGHMARD NDDDLVYLTR LQWDIDRVER DHPDLTLSAT KEMMT
//
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