ID Y0KIB4_9PROT Unreviewed; 525 AA.
AC Y0KIB4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=Meth11DRAFT_1583 {ECO:0000313|EMBL:EUJ10755.1};
OS Methylophilaceae bacterium 11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae.
OX NCBI_TaxID=1101195 {ECO:0000313|EMBL:EUJ10755.1, ECO:0000313|Proteomes:UP000022668};
RN [1] {ECO:0000313|EMBL:EUJ10755.1, ECO:0000313|Proteomes:UP000022668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11 {ECO:0000313|EMBL:EUJ10755.1,
RC ECO:0000313|Proteomes:UP000022668};
RG DOE Joint Genome Institute;
RA Chistoserdova L., Huntemann M., Han J., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., Schaumberg A.,
RA Pati A., Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) 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:EUJ10755.1}.
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DR EMBL; JCKJ01000001; EUJ10755.1; -; Genomic_DNA.
DR AlphaFoldDB; Y0KIB4; -.
DR STRING; 1101195.Meth11DRAFT_1583; -.
DR PATRIC; fig|1101195.3.peg.1543; -.
DR eggNOG; COG4108; Bacteria.
DR Proteomes; UP000022668; 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; cd03689; RF3_II; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000022668}.
FT DOMAIN 10..276
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 87..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 525 AA; 59113 MW; 3F7A225E8CB2CAE7 CRC64;
MSTADLNKIE VRRTFAIISH PDAGKTTLTE KLLWFGGAIQ VAGEVRGRKA ARHATSDWME
LEKQRGISVT SSVMQFPYRE HMINLLDTPG HDDFSEDTYR TLTAVDSAVM VIDSVNGVEA
QTIKLLNVCR MRDTPIVTFI NKLDRESRAP IELLDEIEST LGMECAPMTW PIGMGKTFRG
VYHLHNDEIS FFDPRAEKGT SEIIKGLDNP RLDEVIGRQA EELRIDIELV RGASHSFDKE
RYLSGKQTPV FFGSAINNFG VQSLLDAVVD LSPPPQSRKT ATREIAANES KFSGFVFKIQ
ANMDPKHRDR IAFLRVCSGR FERGMKIKQV ATGKMLSVNN AITFMAQDRT TMDEAYSGDI
IGIPNHGTIK LGDTFTENEN LKFIGIPSFA PEFFRRARIK NPMKMKQLQI GLKQLSEEGA
AQLFRPLLSN DLILGAVGML QFDVVAHRLE HEYGVDMIFE PYDCYTARWL KGSDADLKAI
ADKYGFNVGL DSADDYVYLA PNRVNLQMAQ ERYPDIQFME TREIA
//
