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Database: UniProt
Entry: A0A0A2TDF0_9BACI
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ID   A0A0A2TDF0_9BACI        Unreviewed;       524 AA.
AC   A0A0A2TDF0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=N782_04040 {ECO:0000313|EMBL:KGP73594.1};
OS   Pontibacillus yanchengensis Y32.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP73594.1, ECO:0000313|Proteomes:UP000030147};
RN   [1] {ECO:0000313|EMBL:KGP73594.1, ECO:0000313|Proteomes:UP000030147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y32 {ECO:0000313|EMBL:KGP73594.1,
RC   ECO:0000313|Proteomes:UP000030147};
RX   PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA   Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT   "High quality draft genome sequence of the moderately halophilic bacterium
RT   Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT   genomes.";
RL   Stand. Genomic Sci. 10:93-93(2015).
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:KGP73594.1}.
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DR   EMBL; AVBF01000011; KGP73594.1; -; Genomic_DNA.
DR   RefSeq; WP_036817402.1; NZ_AVBF01000011.1.
DR   AlphaFoldDB; A0A0A2TDF0; -.
DR   STRING; 1385514.N782_04040; -.
DR   eggNOG; COG4108; Bacteria.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000030147; 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; 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:UP000030147}.
FT   DOMAIN          8..274
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   524 AA;  60495 MW;  62B7DB997716853D CRC64;
     MSVKEEMQKR RTFAIISHPD AGKTTLTEKF LLYGNLIRNA GTVKAKKSGK FATSDWMEIE
     KKRGISVTSS VMNFEYEGYQ VNILDTPGHE DFSEDTYRTL TAVDSVIMII DGTKGIEAQT
     LKLFKVCKMR GIPIFTFINK LDREGKDPFD LLKEIEDELG IQTYPMNWPV GMGKRFQGIF
     DRQRDQFIRF SGNEQEIPIP KEELDNYPEL VENETFQAAY EEMELLEEAG EQLDMEAVQQ
     GELTPVFFGS ALAPFGVETF FESFISMAPQ PFPRKASGEL IPPDKEEFSG FIFKIQANMN
     KAHRDRVAFV RVCSGKFERG MNVTLDRTGK TIKIAQTQQF VASSRETAEI AYPGDIIGIY
     DPNVYRIGDT LVEGKNTFHY EELPQFPPEL FKKVTAKNVM KAKQFKKGIE QLVQEGAIQL
     FRGVRNEEYV IGAVGQLQYD VFEYRMKNEY NVDIVLESIG ERMPRWLKEE QVDQKLFDER
     SMLVKDREDN YLALFKNEFS LRWFKDKNPD IELIDLFEVN QYSQ
//
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