ID F6IJP2_9SPHN Unreviewed; 512 AA.
AC F6IJP2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=PP1Y_AT35767 {ECO:0000313|EMBL:CCA94296.1};
OS Novosphingobium sp. PP1Y.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA94296.1, ECO:0000313|Proteomes:UP000009242};
RN [1] {ECO:0000313|EMBL:CCA94296.1, ECO:0000313|Proteomes:UP000009242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX PubMed=21685292; DOI=10.1128/JB.05349-11;
RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA Paolella G., Di Donato A., Salvatore F.;
RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT strain PP1Y.";
RL J. Bacteriol. 193:4296-4296(2011).
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; FR856862; CCA94296.1; -; Genomic_DNA.
DR RefSeq; WP_007012846.1; NC_015580.1.
DR AlphaFoldDB; F6IJP2; -.
DR KEGG; npp:PP1Y_AT35767; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_5; -.
DR OrthoDB; 9802948at2; -.
DR Proteomes; UP000009242; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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 PRINTS; PR01037; TCRTETOQM.
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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00072}; Reference proteome {ECO:0000313|Proteomes:UP000009242}.
FT DOMAIN 3..264
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 12..19
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 512 AA; 56698 MW; C274B7A44BF07A7C CRC64;
MTASRRTFAI ISHPDAGKTT LTEKLLLQGG AIHLAGQVKA RGQARRARSD WMKIEQQRGI
SVTSSVMTFE RTDADGNTIT FNLLDTPGHE DFSEDTYRTL TAVDSAIMVI DAAKGIEPQT
RKLFEVCRLR SVPIITFVNK VDREGRACFD LLDEVADMLA LDVCPMSWPV GMGGLFQGIL
DLKSGKVSRP EGGSKEFLGK VDENVELPEE VAEEIELAQA GYPEFDIEAY RGGDLTPVFF
GSALKNFGVV ELIEAIANFA PPPRPQPTEA GPVDPEHKEV TGFIFKVQAN MDPMHRDRIA
FMRLVSGTFK RGMKLTPSGL GKPIAVHSPI LFFAQDREIA DSAEPGDIIG IPNHGTLRVG
DTLSEKNQIR FTGLPNFAPE ILRRVALRDP TKTKQLRKAL DDLSEEGVIQ VFYPEIGSQW
IVGVVGQLQL DVLISRLEAE YKVEAVLEAS PFDTARWIKG DDKALRDFAD FNKMNLAKDR
DGDPVFMAKS AWDVSYQQER NPDLTFSATK ER
//
