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Database: UniProt
Entry: A0A2S0WD76_9CORY
LinkDB: A0A2S0WD76_9CORY
Original site: A0A2S0WD76_9CORY 
ID   A0A2S0WD76_9CORY        Unreviewed;       529 AA.
AC   A0A2S0WD76;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-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=C3E79_03785 {ECO:0000313|EMBL:AWB83716.1}, DF219_06010
GN   {ECO:0000313|EMBL:PWB99474.1};
OS   Corynebacterium liangguodongii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=2079535 {ECO:0000313|EMBL:AWB83716.1, ECO:0000313|Proteomes:UP000244754};
RN   [1] {ECO:0000313|EMBL:AWB83716.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2184 {ECO:0000313|EMBL:AWB83716.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PWB99474.1, ECO:0000313|Proteomes:UP000245180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2185 {ECO:0000313|EMBL:PWB99474.1,
RC   ECO:0000313|Proteomes:UP000245180};
RA   Liu S., Wang Z., Li J.;
RL   Submitted (APR-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|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; CP026948; AWB83716.1; -; Genomic_DNA.
DR   EMBL; QEEY01000005; PWB99474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0WD76; -.
DR   KEGG; clia:C3E79_03785; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000244754; Chromosome.
DR   Proteomes; UP000245180; 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: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; 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; 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; 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; 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}.
FT   DOMAIN          8..288
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         93..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   529 AA;  57816 MW;  A404547EC711C9BD CRC64;
     MSTLSEAKRR RTFAVIAHPD AGKSTLTEAL ALHAHVISEA GAVHGKGNRK ATVSDWMEME
     KDRGISIASS ALQFEYLPEG ADAAEPYVIN LVDTPGHADF SEDTYRVLSA VDAAVMLIDA
     AKGLEPQTLK LFRVCKARGL PIVTVVNKWD RVGRTPLELV DEIVTEIDLQ PTPLYWPVGE
     AGDFRGLAHI DSDGEADRYI RFIRTAGGST IAPEEHYTPE QAAEHEGETW ETAVEEAELL
     AADGAVHNQE LFEQCVTSPV IFASAMLNFG VHQILDTLCE IAPAPAPRST RALDGDFSGV
     VFKVQAGMDK NHRDTLAFMR VVSGEFDRGM QVTHAQSGRT FSTKYALTVF GRTRDTVETA
     YPGDIIGLVN AGSLAPGDTI FTGAKVQFPP MPQFAPEHFR TLRAKSLGKY KQFRKGLEQL
     DAEGVVQILR NDARGDAAPV MAAVGPMQFE VMQARMDNEY NVETVAEPVP YSVARRTDAE
     SAAELGRQRG VEVFTRSDGE LIALFGDKWK LAFIEKENPQ LTIEPLVAD
//
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