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Database: UniProt
Entry: A0A1G9TJV7_9BACI
LinkDB: A0A1G9TJV7_9BACI
Original site: A0A1G9TJV7_9BACI 
ID   A0A1G9TJV7_9BACI        Unreviewed;       524 AA.
AC   A0A1G9TJV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN05518871_101317 {ECO:0000313|EMBL:SDM47455.1};
OS   Psychrobacillus sp. OK028.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1884359 {ECO:0000313|EMBL:SDM47455.1, ECO:0000313|Proteomes:UP000198927};
RN   [1] {ECO:0000313|Proteomes:UP000198927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK028 {ECO:0000313|Proteomes:UP000198927};
RA   Varghese N., Submissions S.;
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; FNHY01000001; SDM47455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9TJV7; -.
DR   STRING; 1884359.SAMN05518871_101317; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000198927; 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}.
FT   DOMAIN          10..277
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   524 AA;  60103 MW;  187B8807C128D063 CRC64;
     MDIKLQDEIL KRRTFAIISH PDAGKTTITE KLLYFGGAIR DAGTVKGKKS GKFATSDWME
     IEKQRGISVT SSVMQFDYNN CRINILDTPG HQDFSEDTYR TLMAVDSAVM IVDAAKGIEA
     QTLKLFKVCR MRGIPIFTFI NKLDRQGKEP LELMEELEEV LGIQSYAMNW PIGMGKEFLG
     IYDRFNGRIE QFRTEESERF LPLDEEGELA VDHSMKETSY YTQAIEDIML LNEAGNDFDK
     EKVLSGDLTP VFFGSALTNF GVQTFLETYL QFAPTPQPRM TEKEEEINPL NEDFSGFIFK
     IQANMNPAHR DRIAFVRIVS GKFDRGMTVT LARTGKTFKV TQSTQFLADD RETVETAVAG
     DIIGLYDVGN YQIGDTVVGG KKAFTYEKLP QFTPELFVKV TAKNVLKSKH FHKGILQLVQ
     EGAIQYYKTL HTEEIILGAV GQLQFEVFEH RMNNEYNVEV RMEPIGSKVA RWIENEEEVK
     ESMTGPRSML VKDRYDNYVF LFENEFATRW FQDKYEHIKL YNLL
//
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