ID A0A0Q2Y501_9RHOB Unreviewed; 532 AA.
AC A0A0Q2Y501;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ECO:0000313|EMBL:KQI68495.1};
GN ORFNames=AN189_09250 {ECO:0000313|EMBL:KQI68495.1};
OS Loktanella sp. 3ANDIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI68495.1, ECO:0000313|Proteomes:UP000051463};
RN [1] {ECO:0000313|EMBL:KQI68495.1, ECO:0000313|Proteomes:UP000051463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI68495.1,
RC ECO:0000313|Proteomes:UP000051463};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09.";
RL Submitted (SEP-2015) 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 -!- 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:KQI68495.1}.
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; LJAK01000005; KQI68495.1; -; Genomic_DNA.
DR RefSeq; WP_056034499.1; NZ_LJAK01000005.1.
DR AlphaFoldDB; A0A0Q2Y501; -.
DR STRING; 1225657.AN189_09250; -.
DR PATRIC; fig|1225657.3.peg.1894; -.
DR OrthoDB; 9802948at2; -.
DR Proteomes; UP000051463; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051463}.
FT DOMAIN 12..281
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 89..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 532 AA; 59241 MW; 3182045826DCB0C2 CRC64;
MSNRPDLPAE IARRRTFAII SHPDAGKTTL TEKFLLYGGA IQMAGQVRAK GEARRTRSDF
MQMEKDRGIS VSASAMSFDF ERFRFNLVDT PGHSDFSEDT YRTLTAVDAA VMVIDGAKGV
ESQTQKLFEV CRLRDLPILT FCNKMDRESR DTFEIIDEIQ ENLAIDVTPA SWPIGVGREF
MGCYDILRDK LEIMDRADRN KVAASISING LDDPKWSEHV PAHLLEKFRE EIEMAMELLP
KLDPASVLNG SMTPIWFGSA MNSFGVKELM DGIGTYGPEP QIQSAQPRNI APEEPKVAGF
VFKVQANMDP KHRDRVAFVR MASGHFTRGM KLTHVRSKKQ MAVTNPVMFL AADRELAEEA
WAGDIIGIPN HGQLRIGDTL TEGEAIRVSG IPSFAPELLQ NCRAGDPMKA KHLEKALMQF
AEEGAAKVFK PTFGSGFIVG VVGALQFEVL ASRIELEYGL PVRFEGSQFT SARWVHGTKD
AVDKFAAANK QHIALDNDGD TVFLTRLQWD IDRVQRDYPD VTLSATKEMM VG
//