ID A0A1H0GEP3_9GAMM Unreviewed; 529 AA.
AC A0A1H0GEP3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN04487957_103172 {ECO:0000313|EMBL:SDO05342.1};
OS Halomonas shengliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=419597 {ECO:0000313|EMBL:SDO05342.1, ECO:0000313|Proteomes:UP000199075};
RN [1] {ECO:0000313|Proteomes:UP000199075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6444 {ECO:0000313|Proteomes:UP000199075};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNIV01000003; SDO05342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0GEP3; -.
DR STRING; 419597.SAMN04487957_103172; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000199075; 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: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 CDD; cd03689; RF3_II; 1.
DR CDD; cd16259; RF3_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 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..280
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 529 AA; 60067 MW; 09770181E12BB73B CRC64;
MSDANLAREV GLRRTFAIIS HPDAGKTTIT EKMLLFGNAI QLAGSVKSKR DDRHATSDWM
KMEQERGISV TTSVMQFPYG GRIVNLLDTP GHEDFSEDTY RTLTAVDSAL MVIDGAKGVE
ARTIKLMEVC RLRTTPILTF VNKMDRDIRD PIEVMDEVEE VLNIQCAPMT WPIGMGRHFK
GVYHLYNDVI HLYTQGQGSR IPDDRRIEGL DSPEVDEVLG EEQAEELRME VELVRGASHT
FDHDAYLRGE LTPVYFGTAM GNFGVREMLD GFVEYAPPPQ PRETDTRTVE ADDGRFTGFV
FKIQANMDPN HRDRIAFLRV CSGKYEKNMK MRHVRIGKDV KIADALTFMA SDRSQVEEAW
PGDIIGLHNH GTIQIGDTFT QGEDMRFTGI PHFAPELFKR VRLKDPLKMK ALQKGLQQLS
EEGATQVFMP LDNNDLILGA VGTLQFDVVA HRLKEEYKVE AVYEGVNVNT ARWVYCDDAR
KLEEFKRKAS TNLAIDGGGY LTYIAPTRVN LQMTQERWPE IRFQPTREH
//
