RF3_DESVM
ID RF3_DESVM Reviewed; 529 AA.
AC B8DIL5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, 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=DvMF_2372;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) 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: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; CP001197; ACL09313.1; -; Genomic_DNA.
DR RefSeq; WP_015946005.1; NC_011769.1.
DR PDB; 3VQT; X-ray; 1.80 A; A/B/C/D=1-529.
DR PDB; 3VR1; X-ray; 3.00 A; A/B/C/D=1-529.
DR PDBsum; 3VQT; -.
DR PDBsum; 3VR1; -.
DR AlphaFoldDB; B8DIL5; -.
DR SMR; B8DIL5; -.
DR STRING; 883.DvMF_2372; -.
DR PRIDE; B8DIL5; -.
DR EnsemblBacteria; ACL09313; ACL09313; DvMF_2372.
DR KEGG; dvm:DvMF_2372; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_7; -.
DR OMA; GFVFKIH; -.
DR OrthoDB; 164090at2; -.
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; -; 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 PANTHER; PTHR43556; PTHR43556; 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; 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.
FT CHAIN 1..529
FT /note="Peptide chain release factor 3"
FT /id="PRO_1000193520"
FT DOMAIN 10..278
FT /note="tr-type G"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 87..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:3VR1"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:3VQT"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3VQT"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:3VQT"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 408..420
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 423..432
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 443..456
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:3VQT"
FT HELIX 507..516
FT /evidence="ECO:0007829|PDB:3VQT"
FT STRAND 520..527
FT /evidence="ECO:0007829|PDB:3VQT"
SQ SEQUENCE 529 AA; 59251 MW; 34CD14538609B699 CRC64;
MSSRLEREAA RRRTFAIISH PDAGKTTLTE KLLLFGGAIQ MAGSVKARKA ARHATSDWMA
MERERGISVT TSVMQFPYRD RVVNLLDTPG HQDFSEDTYR VLTAVDSALV VIDAAKGVEA
QTRKLMDVCR MRATPVMTFV NKMDREALHP LDVMADIEQH LQIECAPMTW PIGMGSSFKG
TYDLLHKQLH LFSATHGGRI QSGIVIHGAD DPQLDEYLGD QAEQLRMDLA LLEEAGTPFD
EERYLKGELT PVFFGSAINN FGVREMLDMF VEFAPGPQPR PAATRVVEPG EEAFTGVVFK
IQANMDKAHR DRMAFLRICS GTFTRGMRLK HHRTGKDVTV ANATIFMAQD RTGVEEAFPG
DIIGIPNHGT IKIGDTFTES KEVLKFVGIP NFAPEHFRRV RLKNPLKAKQ LQKGLEQLAE
EGAVQLFRPL VNNDYILGAV GVLQFDVIVA RLADEYGVDA VYEGVSTHTA RWVYCEDKKI
FADFQDYHRG ELAVDAEGAL AYLAPNPWRL ESAMERYPKV EFRTTREIS
