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Database: UniProt
Entry: A0A0B3W0A0_9FIRM
LinkDB: A0A0B3W0A0_9FIRM
Original site: A0A0B3W0A0_9FIRM 
ID   A0A0B3W0A0_9FIRM        Unreviewed;       532 AA.
AC   A0A0B3W0A0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=QX51_02065 {ECO:0000313|EMBL:KHS58564.1};
OS   Terrisporobacter othiniensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Terrisporobacter.
OX   NCBI_TaxID=1577792 {ECO:0000313|EMBL:KHS58564.1, ECO:0000313|Proteomes:UP000031189};
RN   [1] {ECO:0000313|EMBL:KHS58564.1, ECO:0000313|Proteomes:UP000031189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=08-306576 {ECO:0000313|EMBL:KHS58564.1,
RC   ECO:0000313|Proteomes:UP000031189};
RA   Lund L.C., Sydenham T.V., Hogh S.V., Skov M.N., Kemp M., Justesen U.S.;
RT   "Draft genome sequence of Terrisporobacter sp. 08-306576, isolated from the
RT   blood culture of a bacteremia patient.";
RL   Submitted (DEC-2014) 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:KHS58564.1}.
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DR   EMBL; JWHR01000027; KHS58564.1; -; Genomic_DNA.
DR   RefSeq; WP_039678253.1; NZ_JWHR01000027.1.
DR   AlphaFoldDB; A0A0B3W0A0; -.
DR   STRING; 1577792.QX51_02065; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000031189; 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; cd04169; RF3; 1.
DR   CDD; cd03689; RF3_II; 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:UP000031189}.
FT   DOMAIN          13..282
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         22..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
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;  59961 MW;  CB25FAD7C9A36216 CRC64;
     MTEQNLNLIN EVKRRRTFAI ISHPDAGKTT LTEKFLLYGG AIREAGSVKS RRSQKHAVSD
     WMEIEKQRGI SVASSVLQFE YDNFCINILD TPGHQDFSED TYRTLMAADS AVMVIDSAKG
     VEAQTKKLFH VCKMRGIPIF TFINKMDRQG KDPFELLEDI ENVLGIRSCP VNWPIGSGKE
     FKGVFNRHKN QVEVFDDGNH GQAIASCITG DPSDEKFTDL LGHDLHEKLL EDIELLDIAG
     DNFDLETILK GELTPVFFGS ALTNFGVEPF LESFLDITTP PTARKSNLGE IDPTSDNFSG
     FIFKIQANMD KNHRDRIAFL RICSGEFEKG MTVNHVQRGK KIKLSQPQQF VAQDRVMIDK
     AYPGDIIGIH DPGIFNIGDT LSAKQSNLQY TGIPQFAPEH FMKVSTKNAL KRKQFVKGVT
     QLSEEGAIQV FKQPNGGMEE LIVGVVGVLQ FEVLEYRLKQ EYGVDVMMYP LPYAHLRWVE
     NDLSKFGKLS MPMDTLLVED KNRNPVVLFA NEWSVRTLAE RNEGLVLRET SL
//
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