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Database: UniProt
Entry: A0A1G8YY13_9CLOT
LinkDB: A0A1G8YY13_9CLOT
Original site: A0A1G8YY13_9CLOT 
ID   A0A1G8YY13_9CLOT        Unreviewed;       530 AA.
AC   A0A1G8YY13;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05660472_00682 {ECO:0000313|EMBL:SDK07769.1};
OS   Natronincola ferrireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Natronincola.
OX   NCBI_TaxID=393762 {ECO:0000313|EMBL:SDK07769.1, ECO:0000313|Proteomes:UP000198718};
RN   [1] {ECO:0000313|EMBL:SDK07769.1, ECO:0000313|Proteomes:UP000198718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18346 {ECO:0000313|EMBL:SDK07769.1,
RC   ECO:0000313|Proteomes:UP000198718};
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}.
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DR   EMBL; FNFP01000001; SDK07769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8YY13; -.
DR   STRING; 393762.SAMN05660472_00682; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000198718; 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   CDD; cd03689; RF3_II; 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:UP000198718}.
FT   DOMAIN          10..279
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   530 AA;  60359 MW;  919E81DF19DD91D1 CRC64;
     MQKDFLKEVR RRRTFAIISH PDAGKTTLTE KLLLYGGAIR LAGSVKSRRA QKHAVSDWME
     IEKQRGISVT SSVMQFDYNN YCINILDTPG HQDFSEDTYR TLMAADSAVM VIDFAKGVEE
     QTKKLFEVCK MRGIPIFTFI NKLDRAGKDP FELMEEIENV LGIRSYPMNW PIGIHGNFKG
     VYNRQKSQIE VFNEGKHGQT VVESVVGDVT DNIFKDLVGE DLHQQLMEEI ELLDVAGDNF
     DLNKVLKGEL TPVFFGSAMT NFGVRPFLEG FLEMTTPPIA RMSNKGEIDP ESNNFTGFIF
     KIQANMNPAH RDRIAFIRIC SGKFQKGMSV NHVRVNKTVK LAQPQQFLAQ DRAVVEEAYP
     GDIIGVHDPG IFNIGDTLCQ DNSKVEYEGI PAFAPEHFAK VYAKDSMKRK QFVKGIEQIS
     EEGAIQVFKR PHAGVEELLV GVVGVLQFEV LQYRLEKEYG VDIKMQSLPY RHVRWVEKEN
     FNYDRFSLTM DSLIAEDKYG KPVVLFENQW SIQKVEERNP GTILKRVSTK
//
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