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Database: UniProt
Entry: A0A1M6N8K0_9CLOT
LinkDB: A0A1M6N8K0_9CLOT
Original site: A0A1M6N8K0_9CLOT 
ID   A0A1M6N8K0_9CLOT        Unreviewed;       530 AA.
AC   A0A1M6N8K0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=SAMN02745248_01318 {ECO:0000313|EMBL:SHJ92022.1};
OS   Hathewaya proteolytica DSM 3090.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX   NCBI_TaxID=1121331 {ECO:0000313|EMBL:SHJ92022.1, ECO:0000313|Proteomes:UP000183952};
RN   [1] {ECO:0000313|EMBL:SHJ92022.1, ECO:0000313|Proteomes:UP000183952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3090 {ECO:0000313|EMBL:SHJ92022.1,
RC   ECO:0000313|Proteomes:UP000183952};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRAD01000009; SHJ92022.1; -; Genomic_DNA.
DR   RefSeq; WP_072903326.1; NZ_FRAD01000009.1.
DR   AlphaFoldDB; A0A1M6N8K0; -.
DR   STRING; 1121331.SAMN02745248_01318; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000183952; 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:UP000183952}.
FT   DOMAIN          9..278
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   530 AA;  60381 MW;  5D2057B10F88D6D4 CRC64;
     MQDLIEKINK RRTFAIISHP DAGKTTLTEK LLLFGGAIRE AGSVKARRSA KHAVSDWMEI
     EKQRGISVTS SVLQFRYDDF YINILDTPGH QDFSEDTYRT LMAADSAVMV VDGAKGVEAQ
     TRKLFQVCSM REIPIFTFVN KLDREIRDPF ELLEDIENEL GIKSYPLNWP IGCGREFKGV
     YNRETETIQL FDGGNHGHSL TNSTFVDFHD ENIEEILGTS FYNKLLEDVE LLDIAGNEFD
     YDKVKDGRLT PVLFGSALTN FGVEPFLKEF LRYSVPPLSR ESDKGEIEAT KPEFSAFVFK
     IQANMNKAHR DRIAFMRICS GKFEKGMEVF HVQGNEKVRL SQPQQFLAQD REIVEEAYAG
     DIIGVFDPGI FSIGDTLCKA SDKFKFHGIP TFAPENFARV KPIDTMKRKQ FDKGITQIAQ
     EGAIQVFKDP FIGIEELIIG VVGVLQFEVL EYRLKNEYNV DIKLEMLPYR NIRWIEKTPV
     KANKLSITSD TKYVKDLKDR DILIFQSDWG IGWALEHNEG LVLSNVGKAE
//
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