GenomeNet

Database: UniProt
Entry: A0A1I4P130_9PROT
LinkDB: A0A1I4P130_9PROT
Original site: A0A1I4P130_9PROT 
ID   A0A1I4P130_9PROT        Unreviewed;       535 AA.
AC   A0A1I4P130;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05421880_109110 {ECO:0000313|EMBL:SFM21482.1};
OS   Nitrosomonas nitrosa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=52442 {ECO:0000313|EMBL:SFM21482.1, ECO:0000313|Proteomes:UP000199561};
RN   [1] {ECO:0000313|EMBL:SFM21482.1, ECO:0000313|Proteomes:UP000199561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm146 {ECO:0000313|EMBL:SFM21482.1,
RC   ECO:0000313|Proteomes:UP000199561};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOUF01000009; SFM21482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4P130; -.
DR   STRING; 52442.SAMN05421880_109110; -.
DR   Proteomes; UP000199561; 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199561}.
FT   DOMAIN          7..275
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   535 AA;  59903 MW;  576361714A2319F6 CRC64;
     MIDQEVQRRR TFAIISHPDA GKTTLTEKLL MFAGAIHIAG SVKARKASRY ATSDWMEIEK
     QRGISVASSV MQMEYRGHVI NLLDTPGHQD FSEDTYRVLT AVDAALMVID AANGVEAQTL
     RLLEVCRARN TPILTFINKM DREVRNPLDL IDEIERTLNM ATIPFTWPIG MGKQFHGVFD
     LRHHSMRVFR PGSDRIEQEG EIIQNLNDDA LASRFGQNFT EARQEIDLIQ GVIPEFDRAA
     FLAGEQTPVF FGSAINNFGV REILDALVDL APPPGARRSL QREVPPIEPK FSGVVFKIQA
     NMNPAHRDRI AFVRVCSGEF KRGMSLKVVR NGKEIRTNTV VSFLSQRREL LDVAYAGDII
     GIPNHGTLQL GDTLTEGEAL HFTGLPFFAP EIFQTVEIAD PMRSKQLKLG LTQLGEEGAI
     QVFRPHIGST LLLGAVGNLQ FEVVTHRLQH EYGVDARIAS AKYQLARWVT ADDPSELQRF
     IDSNAHRIAY DAVDAPTFLA SFAAELSVAQ ENWPAIRFHK MREHAGLVFQ SHMQN
//
DBGET integrated database retrieval system