ID I0XX44_9LEPT Unreviewed; 541 AA.
AC I0XX44;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ECO:0000313|EMBL:EIE03452.1};
GN ORFNames=LEP1GSC185_0001 {ECO:0000313|EMBL:EIE03452.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE03452.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EIE03452.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE03452.1};
RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA Vinetz J.M., Matthias M.A.;
RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT Leptospiral Evolution and Pathogenicity.";
RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
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}.
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:EIE03452.1}.
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DR EMBL; AHOO02000003; EIE03452.1; -; Genomic_DNA.
DR RefSeq; WP_008591971.1; NZ_AHOO02000003.1.
DR AlphaFoldDB; I0XX44; -.
DR PATRIC; fig|1049972.3.peg.15; -.
DR OrthoDB; 9801591at2; -.
DR Proteomes; UP000004889; 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; 2.
DR Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 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 16..285
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"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 541 AA; 60164 MW; 7A376468680107FF CRC64;
MSESAIGQNI IEEETKRRRT FAIIAHPDAG KTTLTEKLLL YGGAIQLAGA VKARKNRKAA
TSDWMEMEKE KGISITSAAL QFEYKNHVLN LLDTPGHEDF SEDTYRTLIA ADTAVMVLDA
GKGVEPQTIK LFKVCRDRGI PIVTFVNKMD RPTKTMFALL DEIEKVLGIA AIPMVWPIGT
GVDFSGVYNR VDKKIYTYDK TPGGSQKSAF QSSGVEDKNL DSMFEDWVLK QFREEVELVE
EGIAAFSLDE FLDSKITPVF FGSAVNNFGI QLFLDHFLEI APPPLYFPLK NGDRLDPVTT
PFSGFVFKVQ ANMNKAHRDR IAFLRVCSGK FERGLNVNHG RLGKAVKLSS SFAFFGQDRN
TVDEAYPGDI IGLVNPGTYS IGDILAIGKV PDLKPLPVFA PEIFATLSCV ETGALKSFRK
GIEQLAEEGI LHLFTSQTVG GGLPVIGAMG QLQFEVFRRR LQDEYSAPTN INILPYQVSC
WLPEEDIPKV PQGSNLVTDS LGRAALLFDS EWEKGYFQKK NPEIRLLDYP TQDVSELNQE
Y
//
