GenomeNet

Database: UniProt
Entry: A0A0A2UXC3_9BACI
LinkDB: A0A0A2UXC3_9BACI
Original site: A0A0A2UXC3_9BACI 
ID   A0A0A2UXC3_9BACI        Unreviewed;       524 AA.
AC   A0A0A2UXC3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=N780_19220 {ECO:0000313|EMBL:KGP91368.1};
OS   Pontibacillus chungwhensis BH030062.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385513 {ECO:0000313|EMBL:KGP91368.1, ECO:0000313|Proteomes:UP000030153};
RN   [1] {ECO:0000313|EMBL:KGP91368.1, ECO:0000313|Proteomes:UP000030153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH030062 {ECO:0000313|EMBL:KGP91368.1,
RC   ECO:0000313|Proteomes:UP000030153};
RA   Wang Q., Wang G.;
RT   "Genome of Pontibacillus chungwhensis.";
RL   Submitted (AUG-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:KGP91368.1}.
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; AVBG01000006; KGP91368.1; -; Genomic_DNA.
DR   RefSeq; WP_036782895.1; NZ_AVBG01000006.1.
DR   AlphaFoldDB; A0A0A2UXC3; -.
DR   STRING; 1385513.N780_19220; -.
DR   eggNOG; COG4108; Bacteria.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000030153; 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   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:UP000030153}.
FT   DOMAIN          8..274
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   524 AA;  60016 MW;  117D9AE33B6A89CA CRC64;
     MSVQNEMKKR RTFAIISHPD AGKTTLTEKF LLFGNLIRES GTVKGKKSGK FATSDWMDIE
     KQRGISVTSS VMNFPYKDYQ VNILDTPGHE DFSEDTYRTL TAVDSVVMII DGTKGIEAQT
     LKLFKVCKMR GIPIFTFINK LDREGRDPFD LLDEIEGELG IETYAMNWPV GMGKRFKGIL
     DRQNEQFVQF TGNETETSIP YDEINDHPEL ADDETFASAF EELELLDGAG VEFSMDAVQQ
     GEQTPVFFGS ALAPFGVRTF FEEFISMAPQ PAPRKASGDM ISPDKEEFSG FIFKIQANMN
     PAHRDRVAFV RVCSGKFERG MNVTLDRTGK SIKLAQTQQF VASSRETIQE AYAGDIIGIY
     DPNVYRIGDT LVEGKETFHF EELPQFPPEV FKKVVVENVM KSKQFKKGLE QLVQEGAIQL
     FRSLRSDEYI IGAVGQLQYE VFEYRMKNEY NVGVRFEDIG ERIPRWLKSE QVDRSKFDDR
     SLLVKDREEN YLALFKNDFS LRWFQDKNPD IDLIDLFEVN QYSQ
//
DBGET integrated database retrieval system