RF3_STRMK
ID RF3_STRMK Reviewed; 534 AA.
AC B2FR00;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Smlt3637;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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}.
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DR EMBL; AM743169; CAQ47053.1; -; Genomic_DNA.
DR RefSeq; WP_005410681.1; NC_010943.1.
DR PDB; 7SIQ; X-ray; 2.95 A; A=1-534.
DR PDBsum; 7SIQ; -.
DR AlphaFoldDB; B2FR00; -.
DR SMR; B2FR00; -.
DR STRING; 522373.Smlt3637; -.
DR EnsemblBacteria; CAQ47053; CAQ47053; Smlt3637.
DR GeneID; 61467118; -.
DR KEGG; sml:Smlt3637; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_6; -.
DR OMA; TPASWPI; -.
DR OrthoDB; 164090at2; -.
DR Proteomes; UP000008840; Chromosome.
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; 3.30.70.3280; -; 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..534
FT /note="Peptide chain release factor 3"
FT /id="PRO_1000092504"
FT DOMAIN 9..278
FT /note="tr-type G"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:7SIQ"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:7SIQ"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 394..403
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 407..419
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 442..453
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 477..484
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:7SIQ"
FT HELIX 506..515
FT /evidence="ECO:0007829|PDB:7SIQ"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:7SIQ"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:7SIQ"
SQ SEQUENCE 534 AA; 58939 MW; 21103D8586C32D6F CRC64;
MSEVANEASR RRTFAIISHP DAGKTTLTEK LLLFGGAIQM AGSVKGRKAA RHATSDWMAL
EKERGISVTS SVMQFPYEDK IVNLLDTPGH ADFGEDTYRV LTAVDSALMV IDVAKGVEER
TIKLMEVCRL RDTPIMTFIN KLDREGKDPI ELLDEVETVL GIQCAPVTWP IGMGQRLKGV
VHLLTGEVHL YEPGRNFTRQ DSTIFPSIDA PGLAEKIGAQ MLADLRDELE LVQGASHPFD
LEAYRAGKQT PVFFGSGVNN FGVQPLLDFF VEHAPSPQAR STTGREIAPE ENKLTGFVFK
IQANMDPQHR DRVAFMRVCS GRFSAGMKTF HVRTGKEMKL ANALTFMASD REIAAEAWPG
DVIGIHNHGT ISIGDTFTEG EAVTFTGIPN FAPELFRRAR LRDPLKLKQL QKGLAQLSEE
GATQFFRPLT SNDLILGAVG VLQFDVAAYR LKDEYGVEAT FEPVSVTTAR WVHCSNEKKL
EEFREKNALN LALDAAGHLV YLAPTRVNLQ LAQERSPDVR FSATREAAHT VSVG
