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Database: UniProt
Entry: A0A2R3JT22_9LACO
LinkDB: A0A2R3JT22_9LACO
Original site: A0A2R3JT22_9LACO 
ID   A0A2R3JT22_9LACO        Unreviewed;       525 AA.
AC   A0A2R3JT22;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=C5Z26_00735 {ECO:0000313|EMBL:AVK62752.1};
OS   Lactobacillus sp. CBA3606.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=2099789 {ECO:0000313|EMBL:AVK62752.1, ECO:0000313|Proteomes:UP000238064};
RN   [1] {ECO:0000313|EMBL:AVK62752.1, ECO:0000313|Proteomes:UP000238064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBA3606 {ECO:0000313|EMBL:AVK62752.1,
RC   ECO:0000313|Proteomes:UP000238064};
RA   Jung M.Y.;
RT   "Complete genome sequence of Lactobacillus sp. CBA3606.";
RL   Submitted (FEB-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; CP027194; AVK62752.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R3JT22; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000238064; 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   CDD; cd03689; RF3_II; 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}.
FT   DOMAIN          11..279
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   525 AA;  59570 MW;  9C77CAA809422D55 CRC64;
     MNKSELAAAV DTRRTFAIIS HPDAGKTTIT EQMLLFGGVV RQAGTVKARK SGSFAKSDWM
     EIEKKRGISV TSSVMQFDYD GKRINILDTP GHEDFSEDTY RTLMAVDSAI MVIDSAKGIE
     PQTKKLFQIC KMRGIPIFTF MNKLDRDGRE PLDLLNEVEE VLGIETYPMN WPIGMGKGLK
     GLYDRYNHRI ELYHNEAHGR TFLPLNEAGE VTVENDLTKD SIYRDVLDEM ELIEAAGNEF
     DEQKIADGDM TPVFFGSALT NFGVETFLKT YLKYAPKPNV HKTRADTIIK PTDDEFSAFV
     FKIQANMNPN HRDRIAFVRI CSGEFDRGMD VFLQRTGKKM RLNNSTQFMA DTRETVETAV
     AGDIVGLYDT GNFQIGDTIY DGKQAIQFEK LPQFTPELFM RVTAKNVMKQ KSFHKGIEQL
     VQEGAVQLYT SYSTGDYVLG AVGQLQFEVF KFRMQNEYNS EVVMEPMGNK TARWIDPAQL
     DEKMSSSRNL LVKDQAGAPL FLFENAFAER WFSEKYPDVK LTAKL
//
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