ID A0A2A7MLY8_9CLOT Unreviewed; 531 AA.
AC A0A2A7MLY8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CQ394_12820 {ECO:0000313|EMBL:PEG32533.1};
OS Clostridium neonatale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG32533.1, ECO:0000313|Proteomes:UP000220840};
RN [1] {ECO:0000313|EMBL:PEG32533.1, ECO:0000313|Proteomes:UP000220840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG32533.1,
RC ECO:0000313|Proteomes:UP000220840};
RA Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT "Effective Description of Clostridium neonatale sp. nov. linked to
RT necrotizing enterocolitis in neonates and a clarification of species
RT assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT Rainey 2016.";
RL Submitted (OCT-2017) 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:PEG32533.1}.
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DR EMBL; PDCJ01000001; PEG32533.1; -; Genomic_DNA.
DR RefSeq; WP_058296677.1; NZ_PDCJ01000001.1.
DR AlphaFoldDB; A0A2A7MLY8; -.
DR STRING; 137838.GCA_001458595_04054; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000220840; 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: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:UP000220840}.
FT DOMAIN 9..278
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 531 AA; 60106 MW; F3A8BBE7C3E03C0C CRC64;
MADYKQEIEK RRTFAIISHP DAGKTTLTEK FLLYGGAIRL AGSVKARKAS KHAVSDWMEI
EKQRGISVTS SVMQFNYGGH CINILDTPGH QDFSEDTYRT LMAADSAVMV VDAAKGIEDQ
TRKLFHVASL REMPIFTFIN KMDREAKDPF GLLDDIENEL GIKTYPMNWP IGSGKEFKGV
YERDNNRIIA FNGGNHGQNE VEAIEGTPDD PKFREILGEA LHDKLMEDIE LLDIAGDELD
IEAVRKGELT PVFFGSALTN FGVEPFLEHF LEMTTSPLPR NSSEGLIDPF DKNFSAFVFK
IQANMNKAHR DRIAFMRICS GEFNKGEDVY HVQGGKKIKL AQPQQFMAEN REIVEEAYAG
DIIGVFDPGI FSIGDTLCSP SKKFKFEGIP TFSPEHFAKV RPVDTMKRKQ FIKGVTQIAQ
EGAIQVFKEI HIGMEEIIVG VVGVLQFEVL EYRLKNEYNV DVKMERNSYR YVRWIENKDV
DMDSLNLTSD TRKVKDIKDR NLLIFQNDWG ISWALDHNDG LILSDVGKSE A
//
