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Database: UniProt
Entry: A0A2S1GYK6_9BACI
LinkDB: A0A2S1GYK6_9BACI
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ID   A0A2S1GYK6_9BACI        Unreviewed;       523 AA.
AC   A0A2S1GYK6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=DCE79_03395 {ECO:0000313|EMBL:AWE06486.1};
OS   Lysinibacillus sp. 2017.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=2169540 {ECO:0000313|EMBL:AWE06486.1, ECO:0000313|Proteomes:UP000244315};
RN   [1] {ECO:0000313|Proteomes:UP000244315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2017 {ECO:0000313|Proteomes:UP000244315};
RA   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|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; CP029002; AWE06486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S1GYK6; -.
DR   KEGG; lyz:DCE79_03395; -.
DR   Proteomes; UP000244315; Chromosome.
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   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:UP000244315}.
FT   DOMAIN          8..275
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   523 AA;  59809 MW;  00E5EEC3078456E6 CRC64;
     MTLEQDILSR RTFAIISHPD AGKTTITEKL LLFGGAIRDA GTVKGKKSGK FATSDWMEIE
     KQRGISVTSS VMQFDYSDCR VNILDTPGHQ DFSEDTYRTL MAVDSAVMIV DAAKGIEAQT
     LKLFKVCKMR GIPIFTFINK LDRQGKEPLE LIEELEEVLG ISAYPMNWPI GMGKEFLGIY
     DRYNNRIEQF RTDENERYLP VDEKGHLAVE HPMKVTSYYT QAMDDIELLN EAGNAYSEEK
     IRRGELTPVF FGSALTNFGV QTFLDTYLKF APTPQPRITE DEQYIDPVEY NEFSGFIFKI
     QANMNPAHRD RIAFVRIVSG KFERGMNMTL ARTGKSFKVT QSTQFLADDR EIVNEAVAGD
     IIGLYDTGTY QIGDTVVGGK KGFNFEKLPQ FTPEIFMRVS AKNVMKGKQF QKGVLQLVQE
     GAIQYFKTLH TEEIILGAVG QLQFEVFQHR MIGEYNVEVT MQPIGSKIAR WVENEEDVKD
     SMHSQRSMLV KDRFDKKVFL FENEFAMRWF ADKNEHIKLY SLL
//
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