ID A0A1J5TS29_9GAMM Unreviewed; 523 AA.
AC A0A1J5TS29;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=BGC33_07875 {ECO:0000313|EMBL:OIR23714.1}, MS2017_1644
GN {ECO:0000313|EMBL:AYQ57326.1}, THERMOS_1993
GN {ECO:0000313|EMBL:CAB5504626.1};
OS Bathymodiolus thermophilus thioautotrophic gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2360 {ECO:0000313|EMBL:OIR23714.1, ECO:0000313|Proteomes:UP000182798};
RN [1] {ECO:0000313|Proteomes:UP000182798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAT/CrabSpa'14 {ECO:0000313|Proteomes:UP000182798};
RA Ponnudurai R., Kleiner M., Sayavedra L., Thuermer A., Felbeck H.,
RA Schlueter R., Schweder T., Markert S.;
RT "Genome Sequence of Bathymodiolus thermophilus sulfur-oxidizing gill
RT endosymbiont.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIR23714.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BAT/CrabSpa'14 {ECO:0000313|EMBL:OIR23714.1};
RX PubMed=28878861; DOI=10.1186/s40793-017-0266-y;
RA Ponnudurai R., Sayavedra L., Kleiner M., Heiden S.E., Thurmer A.,
RA Felbeck H., Schluter R., Sievert S.M., Daniel R., Schweder T., Markert S.;
RT "Genome sequence of the sulfur-oxidizing Bathymodiolus thermophilus gill
RT endosymbiont.";
RL Stand. Genomic Sci. 12:50-50(2017).
RN [3] {ECO:0000313|EMBL:AYQ57326.1, ECO:0000313|Proteomes:UP000278334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR9N {ECO:0000313|EMBL:AYQ57326.1,
RC ECO:0000313|Proteomes:UP000278334};
RA Won Y.-J.;
RT "Genome sequence of the bacterial symbiont EPR9N from a vent mussel
RT Bathymodiolus thermophilus.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CAB5504626.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B thermophilus SOXS {ECO:0000313|EMBL:CAB5504626.1};
RA Petersen J., Sayavedra L.;
RL Submitted (MAY-2020) 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}.
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DR EMBL; CP024634; AYQ57326.1; -; Genomic_DNA.
DR EMBL; CAESAQ020000078; CAB5504626.1; -; Genomic_DNA.
DR EMBL; MIQH01001205; OIR23714.1; -; Genomic_DNA.
DR RefSeq; WP_071565369.1; NZ_MIQH01001205.1.
DR AlphaFoldDB; A0A1J5TS29; -.
DR KEGG; bthg:MS2017_1644; -.
DR Proteomes; UP000182798; Unassembled WGS sequence.
DR Proteomes; UP000278334; Chromosome.
DR Proteomes; UP000643672; 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; 2.
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 6..275
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 523 AA; 58275 MW; FE55819ABFAD9F69 CRC64;
MISEISKRRT FAIISHPDAG KTTVTEKLLL YAGAIKTAGS VKARKSNTHA TSDWMEMEKE
RGISITSSIM QFEYDKHVIN LLDTPGHEDF SEDTYRTLTA VDSALMVIDV AKGVEMRTIK
LMEVCRLRDT PILTFINKLD REGKEPIDLL DEVETVLNIE CAPITWPIGM GKRFKGVVHL
LEDKIYLYEA GKNSEIGENI IIDGINNPQL DEILGADEVL EMREEVELIR ETTTPFDVDK
FLAGQQTPVF FGSAISNFGI QNLLDGFLEY APTPKNRESD IREVKPEEDK LTGFVFKIQA
NMDPKHHDRL AFMRLVSGQY KKGMKVLQVS TGKQIKIANA VTFMSRERSS AEVAYAGDVI
GIHNHGGISI GDTFTQGEKL SFQGIPNFAP ELFRRAVLKD PLKAKALQKG LDQLSEEGAT
QVFRPIINNS QILGAVGILQ FDVVAHRLKY EYGVDCQFET INIATARWIT GSDKDIEQLK
AKAGNNVAVD SAGVLTYLAP STVNLQLTIE RHPNLVFSAT REH
//
