ID A0A0R3CSH6_9BRAD Unreviewed; 540 AA.
AC A0A0R3CSH6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KRQ00714.1};
GN ORFNames=AOQ71_37415 {ECO:0000313|EMBL:KRQ00714.1};
OS Bradyrhizobium manausense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=989370 {ECO:0000313|EMBL:KRQ00714.1, ECO:0000313|Proteomes:UP000051936};
RN [1] {ECO:0000313|EMBL:KRQ00714.1, ECO:0000313|Proteomes:UP000051936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3351 {ECO:0000313|EMBL:KRQ00714.1,
RC ECO:0000313|Proteomes:UP000051936};
RA De Araujo J.L., Zilli J.E.;
RT "Draft Genome Sequence of Bradyrhizobium manausense Strain BR 3351T, a
RT Novel Symbiotic Nitrogen-Fixing Alphaproteobacterium Isolated from
RT Brazilian Amazon Rain Forest.";
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:KRQ00714.1}.
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DR EMBL; LJYG01000112; KRQ00714.1; -; Genomic_DNA.
DR RefSeq; WP_057758030.1; NZ_LJYG01000112.1.
DR AlphaFoldDB; A0A0R3CSH6; -.
DR STRING; 989370.AOQ71_37415; -.
DR OrthoDB; 9802948at2; -.
DR Proteomes; UP000051936; 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 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00072}.
FT DOMAIN 22..287
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 99..103
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 540 AA; 59557 MW; CB334C6FDDA8D6CF CRC64;
MSDIAATTAE SPARSPLAAE VSRRRTFAII SHPDAGKTTL TEKLLLFGGA INLAGQVKAK
GERRNTRSDW MKIERERGIS VVTSVMTFEF EGLVFNLLDT PGHEDFSEDT YRTLTAVDSA
VMVIDAAKGI EARTRKLFEV CRLRDIPIIT FINKMDRESR DVFELLDEIE KTLALDTTPM
TWPVGRGRDF LGTYDVIDGG VRLLEGGGAK TGAAQQIEIA ELAKLNANLD ASAVKEELEL
VTEASKPFEL EAFREGHLTP VYFGSALRNF GVGDLLEGLG KFAPEPRAQD SDQRKVEATD
PRMSAFVFKI QANMDPNHRD RIAFARLCSG KLSRGMKAKL VRTGKSMPLS SPQFFFAQDR
SVADEAFAGD VVGIPNHGTL RIGDTLTEGE DFNFVGVPSF APEIVRRVRL TDAMKAKKLK
EALQQMSEEG VVQVFRPRDG APALVGVVGA LQLDVLKARL EAEYSLPVEF EVSEFQLARW
VSSEDRKKLD AFIAANTSSI ADDVDGDPVY LARNEFYLGY TKERAEGIEF TNVKDVKKKG
//
