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Database: UniProt
Entry: A0A3N1DBW1_9ACTN
LinkDB: A0A3N1DBW1_9ACTN
Original site: A0A3N1DBW1_9ACTN 
ID   A0A3N1DBW1_9ACTN        Unreviewed;       534 AA.
AC   A0A3N1DBW1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=EDD29_8753 {ECO:0000313|EMBL:ROO91011.1};
OS   Actinocorallia herbida.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinocorallia.
OX   NCBI_TaxID=58109 {ECO:0000313|EMBL:ROO91011.1, ECO:0000313|Proteomes:UP000272400};
RN   [1] {ECO:0000313|EMBL:ROO91011.1, ECO:0000313|Proteomes:UP000272400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44254 {ECO:0000313|EMBL:ROO91011.1,
RC   ECO:0000313|Proteomes:UP000272400};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (NOV-2018) 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|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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:ROO91011.1}.
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DR   EMBL; RJKE01000001; ROO91011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1DBW1; -.
DR   Proteomes; UP000272400; 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   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; 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; 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; 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:UP000272400}.
FT   DOMAIN          16..281
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         93..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   534 AA;  57677 MW;  6D45B92A0E303D2B CRC64;
     MSTVKAKIDE VSAEAARRRT FAVISHPDAG KSTLTEALAV QAAAISTAGA VHGKGDRAGV
     TSDWMEMERS RGISITSSVL RFDYHGALLN LLDTPGHADF SEDTYRVLSA VDGAVMLLDS
     AKGLEAQTLK LFDVCKHGNV PILTFVNKWD RPGREPLELL DEVEQRIGLH AAPLNWPVGI
     AGDFRGLISR ADGSFTKFVP GIGGAKAQAV RMSAEDAAAE LGDVWETAME ELTLLTEIGA
     ELDEEAFTGG ISTPVLFGAA LPQFGVSALL DALTTYAPPP AARKDAEGDR RPLDTPFSGQ
     VFKVQAGMDK AHRDSLAFIR VCSGRFERGM TLTMGSTGRG LVTKHAQTVF GRDRTTVDTA
     YPGDVIGLPN THGLTVGESL YEGSPAVSYP AIPAFAPEHF MVCRAKDVGK YKQFRRGIEQ
     LDSEGAVQVL RSDIRGDQAP VLAAVGPLQF EVVAHRMEHE FNSPVNLNGL DFSECRLTDA
     ESAEQLAKMR GVEVFKRSLT GDLVVLFADK WRLRAIEREH PDLKIEQMLA AGQY
//
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