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Database: UniProt
Entry: A0A0Q2Y501_9RHOB
LinkDB: A0A0Q2Y501_9RHOB
Original site: A0A0Q2Y501_9RHOB 
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}.
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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
//
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