RF3_COXBU
ID RF3_COXBU Reviewed; 525 AA.
AC Q83DC7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Peptide chain release factor 3 {ECO:0000255|HAMAP-Rule:MF_00072};
DE Short=RF-3 {ECO:0000255|HAMAP-Rule:MF_00072};
GN Name=prfC {ECO:0000255|HAMAP-Rule:MF_00072}; OrderedLocusNames=CBU_0811;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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:0000255|HAMAP-Rule:MF_00072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00072}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016828; AAO90345.1; -; Genomic_DNA.
DR RefSeq; NP_819831.1; NC_002971.3.
DR RefSeq; WP_005772589.1; NC_002971.4.
DR PDB; 3TR5; X-ray; 2.11 A; A/B/C/D=1-525.
DR PDBsum; 3TR5; -.
DR AlphaFoldDB; Q83DC7; -.
DR SMR; Q83DC7; -.
DR STRING; 227377.CBU_0811; -.
DR DNASU; 1208704; -.
DR EnsemblBacteria; AAO90345; AAO90345; CBU_0811.
DR GeneID; 1208704; -.
DR KEGG; cbu:CBU_0811; -.
DR PATRIC; fig|227377.7.peg.796; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_6; -.
DR OMA; GFVFKIH; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016150; F:translation release factor activity, codon nonspecific; IBA:GO_Central.
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 GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR CDD; cd04169; RF3; 1.
DR Gene3D; 3.30.70.3280; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; 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 PANTHER; PTHR43556; PTHR43556; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF16658; RF3_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 1.
DR TIGRFAMs; TIGR00503; prfC; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..525
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000210937"
FT DOMAIN 8..276
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3TR5"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:3TR5"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3TR5"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 218..233
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:3TR5"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 405..417
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 440..453
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 475..484
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:3TR5"
FT HELIX 504..513
FT /evidence="ECO:0007829|PDB:3TR5"
FT STRAND 517..524
FT /evidence="ECO:0007829|PDB:3TR5"
SQ SEQUENCE 525 AA; 59477 MW; 61231CD9F841F7AC CRC64;
MSVEKQTAMR RTFAIISHPD AGKTTLTEKL LLFGGAIQLA GTIKSRKAAR HATSDWMELE
KQRGISVTTS VMQFPYKDYL INLLDTPGHA DFTEDTYRTL TAVDSALMVI DAAKGVEPRT
IKLMEVCRLR HTPIMTFINK MDRDTRPSIE LLDEIESILR IHCAPVTWPI GMGKYFKGIY
HLIEDAIYLY QPGKHERVGE SERIEGINNP ELDKKLGDLA SELRNEIELV KGASHPFERE
GYLKGELTPI FFGSAINNFG VGELLDAFVK EAPPPQGRET NSRLVKPEEE KFSGFVFKIQ
ANMDPGHRDR IAFLRIASGQ YQKGMKAYHV RLKKEIQINN ALTFMAGKRE NAEEAWPGDI
IGLHNHGTIQ IGDTFTQGER FKFTGIPNFA SELFRLVRLK DPLKQKALLK GLTQLSEEGA
TQLFRPLDSN ELILGAVGLL QFDVVAYRLE NEYNVKCVYE SVNVVTARWV ICDDKAVLER
FNQEQSRNLA YDGGGHLTYL APSRVNLEIT MEKWPEIQFS ETREH