ID A0A1H9TSC4_9CORY Unreviewed; 543 AA.
AC A0A1H9TSC4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05661109_01530 {ECO:0000313|EMBL:SER99934.1};
OS Corynebacterium cystitidis DSM 20524.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121357 {ECO:0000313|EMBL:SER99934.1, ECO:0000313|Proteomes:UP000198929};
RN [1] {ECO:0000313|EMBL:SER99934.1, ECO:0000313|Proteomes:UP000198929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20524 {ECO:0000313|EMBL:SER99934.1,
RC ECO:0000313|Proteomes:UP000198929};
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|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}.
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DR EMBL; FOGQ01000006; SER99934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9TSC4; -.
DR STRING; 1121357.SAMN05661109_01530; -.
DR Proteomes; UP000198929; 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}.
FT DOMAIN 8..285
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 92..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 543 AA; 59785 MW; 0A4482CA43D3B091 CRC64;
MSTLSEAKRR RTFAVIAHPD AGKSTLTEAL ALHAHVISEA GATHGKGNRK ATVSDWMEME
KDRGISIASS ALQFEYQPEG YEGEPYVINL VDTPGHADFS EDTYRVLSAV DAAVMLIDAA
KGLEPQTLKL FRVCKARGLP IITVINKWDR IGREPLDLVE EIVTEIDLQP TPLYWPVGEA
GDFRGLAHVD DNGEVDNYVH FTRTAGGSTI APETFYSPDE AEAKEGDAWE TAVMEAELLA
GDGAVHDQQM FEQCITSPLI FASAMLNFGV HQILDTLCAI APAPEGRASD PKAVEASTSA
MDRFRELDDE FSGVVFKVQA GMDKSHRDTL AFMRVVSGEF DRGMQVTHAQ SERSFSTKYA
LTVFGRTRDT VETAYPGDII GLVNAGSLAP GDTIYAGKKV QFPPMPQFAP EYFQTLRAKS
LGKYKQFRKA LEQLDAEGVV QILRNDLRGD AAPVMAAVGP MQFEVMQARM ENEYNVETVT
ESVPYSVARR TDAESADELG RQRGVEIFTR TDGELIALFG DKWKLAFIER EHPELTMEPL
VAD
//
