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Database: UniProt
Entry: K9B5R2_9MICO
LinkDB: K9B5R2_9MICO
Original site: K9B5R2_9MICO 
ID   K9B5R2_9MICO            Unreviewed;       530 AA.
AC   K9B5R2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=C272_00300 {ECO:0000313|EMBL:EKU49130.1};
OS   Brevibacterium casei S18.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU49130.1, ECO:0000313|Proteomes:UP000009879};
RN   [1] {ECO:0000313|EMBL:EKU49130.1, ECO:0000313|Proteomes:UP000009879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S18 {ECO:0000313|EMBL:EKU49130.1,
RC   ECO:0000313|Proteomes:UP000009879};
RA   Sharma R., Singh A., Jangir P.K.;
RT   "Genome Sequence of Brevibacterium casei S18.";
RL   Submitted (SEP-2012) 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}.
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:EKU49130.1}.
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DR   EMBL; AMSP01000001; EKU49130.1; -; Genomic_DNA.
DR   RefSeq; WP_009374561.1; NZ_AMSP01000001.1.
DR   AlphaFoldDB; K9B5R2; -.
DR   GeneID; 61005147; -.
DR   PATRIC; fig|1229781.4.peg.59; -.
DR   eggNOG; COG4108; Bacteria.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000009879; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009879}.
FT   DOMAIN          16..282
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   530 AA;  58310 MW;  50CA63375526DA83 CRC64;
     MTSGRYSDKE IRTQAARRRT FAVISHPDAG KSTTTEALAL HARAIGQAGA THGKAGRRAT
     VSDWMQMEQD RGISISSAAL QFEYRDAVFN LVDTPGHADF SEDTYRVLSA VDCAVMLIDA
     AKGLESQTMK LFEVCAHRNI PIITVVNKWD RPGLDALALM DEVQQRTGLL PTPITWPVGQ
     SGDFRGVLDR ITGEYTKYTR TDGGATIAGE ETFAPEAAAE LEGEAWTTAV DESELLDMED
     QNHDQETFLA GKSTPVMFAS AVLNFGIHKL LDTLVDLAPA AEAREDKESA PRDVAAPFSG
     FVFKVQAGMD SNHRDRLAYI RVCSGVFERG SVLTHSATGK PFATKYAQQV FGRDRDVVDE
     AFPGDVVGLV NASALRVGDS LYLDKKVEFP GIPTFSPEHF MVIRAKDSSK YKQFRRGIEQ
     LDHEGVIQVL RSDLRGDQAP VLGAVGPMQF EVAEDRMTNE FNAPCSLERL NFSLARRTTP
     ECVPTLARER NVEVLSRSDG ELLALFSDRW RLQGVEKNHP DLVLEPLVVS
//
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