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Database: UniProt
Entry: A0A0A5GI63_9BACI
LinkDB: A0A0A5GI63_9BACI
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ID   A0A0A5GI63_9BACI        Unreviewed;       524 AA.
AC   A0A0A5GI63;
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=N781_13690 {ECO:0000313|EMBL:KGX92931.1};
OS   Pontibacillus halophilus JSM 076056 = DSM 19796.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX92931.1, ECO:0000313|Proteomes:UP000030528};
RN   [1] {ECO:0000313|EMBL:KGX92931.1, ECO:0000313|Proteomes:UP000030528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX92931.1,
RC   ECO:0000313|Proteomes:UP000030528};
RA   Huang J., Wang G.;
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:KGX92931.1}.
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DR   EMBL; AVPE01000004; KGX92931.1; -; Genomic_DNA.
DR   RefSeq; WP_026800007.1; NZ_AVPE01000004.1.
DR   AlphaFoldDB; A0A0A5GI63; -.
DR   STRING; 1385510.GCA_000425205_01571; -.
DR   eggNOG; COG4108; Bacteria.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000030528; 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:UP000030528}.
FT   DOMAIN          8..272
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;  59904 MW;  EC13E99686B51B69 CRC64;
     MTIQDEVNKR RTFAIISHPD AGKTTLTEKF LLFGNLIRES GTVKGKKSGK FATSDWMDIE
     KKRGISVTSS VMHFDYEGYA VNILDTPGHE DFSEDTYRTL TAVDSVVMVI DGTKGIEPQT
     IKLFKVCKMR GIPIFTFINK LDREGKDPFE LLDEIEEVLG IETYAMNWPA GMGKRFLGIF
     DRLEDRFIQY TGNEEENVIP GSEYDQYPEL TESGTFQSAK EEVELLQEAG EPYSMEAIQN
     GEQTPVFFGS ALAPFGVESF FNTFLNMAPS PAPRKASGDL VAPEKEQFSG FIFKIQANMN
     PAHRDRVAFV RVCSGKFERG MNVTLHRTGK AFKVSQTQQF VASSRETVEE AYAGDIIGIY
     DPNVYRIGDT LVEGKNTFEY EELPQFPPEL FKRATVKNVM KSKQFKKGME QLVQEGAIQL
     FRGAKMDEYI VGAVGELQYD VFEYRLKNEY NVEVIFETIG ERIPRWLKEE QVDYSLFDDR
     SKLVKDREGN HLALFKNDFS LRWFKDKHPD IELIDLFESN EYSQ
//
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