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Database: UniProt
Entry: B8DIL5
LinkDB: B8DIL5
Original site: B8DIL5 
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   29-OCT-2014, entry version 40.
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};
GN   OrderedLocusNames=DvMF_2372;
OS   Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Miyazaki F / DSM 19637;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hazen T.C., 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
CC       complexes and stimulates activities of RF-1 and RF-2. It binds
CC       guanine nucleotides and has strong preference for UGA stop codons.
CC       It may interact directly with the ribosome. The stimulation of RF-
CC       1 and RF-2 is significantly reduced by GTP and GDP, but not by
CC       GMP. {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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00072}.
CC   -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding)
CC       domain. {ECO:0000305}.
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DR   EMBL; CP001197; ACL09313.1; -; Genomic_DNA.
DR   RefSeq; YP_002436781.1; 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   ProteinModelPortal; B8DIL5; -.
DR   SMR; B8DIL5; 5-527.
DR   STRING; 883.DvMF_2372; -.
DR   EnsemblBacteria; ACL09313; ACL09313; DvMF_2372.
DR   GeneID; 7174306; -.
DR   KEGG; dvm:DvMF_2372; -.
DR   PATRIC; 21775133; VBIDesVul86729_2571.
DR   eggNOG; COG4108; -.
DR   HOGENOM; HOG000236725; -.
DR   KO; K02837; -.
DR   OMA; WMEMERE; -.
DR   OrthoDB; EOG6677Q1; -.
DR   BioCyc; DVUL883:GCJ5-2440-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00072; Rel_fac_3; 1.
DR   InterPro; IPR000795; EF_GTP-bd_dom.
DR   InterPro; IPR009022; EFG_III-V.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004548; PrfC.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 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; Complete proteome; Cytoplasm; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    529       Peptide chain release factor 3.
FT                                /FTId=PRO_1000193520.
FT   DOMAIN       10    278       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00072}.
FT   NP_BIND      87     91       GTP. {ECO:0000255|HAMAP-Rule:MF_00072}.
FT   NP_BIND     141    144       GTP. {ECO:0000255|HAMAP-Rule:MF_00072}.
FT   HELIX         4     10       {ECO:0000244|PDB:3VQT}.
FT   STRAND       12     18       {ECO:0000244|PDB:3VQT}.
FT   HELIX        25     35       {ECO:0000244|PDB:3VQT}.
FT   HELIX        39     47       {ECO:0000244|PDB:3VQT}.
FT   HELIX        56     62       {ECO:0000244|PDB:3VR1}.
FT   TURN         70     72       {ECO:0000244|PDB:3VQT}.
FT   STRAND       73     78       {ECO:0000244|PDB:3VQT}.
FT   STRAND       81     86       {ECO:0000244|PDB:3VQT}.
FT   HELIX        91     93       {ECO:0000244|PDB:3VQT}.
FT   HELIX        96    103       {ECO:0000244|PDB:3VQT}.
FT   STRAND      106    113       {ECO:0000244|PDB:3VQT}.
FT   TURN        114    116       {ECO:0000244|PDB:3VQT}.
FT   HELIX       120    131       {ECO:0000244|PDB:3VQT}.
FT   STRAND      136    141       {ECO:0000244|PDB:3VQT}.
FT   HELIX       150    161       {ECO:0000244|PDB:3VQT}.
FT   STRAND      163    173       {ECO:0000244|PDB:3VQT}.
FT   HELIX       175    177       {ECO:0000244|PDB:3VQT}.
FT   STRAND      180    183       {ECO:0000244|PDB:3VQT}.
FT   TURN        184    187       {ECO:0000244|PDB:3VQT}.
FT   STRAND      188    191       {ECO:0000244|PDB:3VQT}.
FT   HELIX       213    218       {ECO:0000244|PDB:3VQT}.
FT   HELIX       219    221       {ECO:0000244|PDB:3VQT}.
FT   HELIX       222    235       {ECO:0000244|PDB:3VQT}.
FT   HELIX       241    245       {ECO:0000244|PDB:3VQT}.
FT   STRAND      248    254       {ECO:0000244|PDB:3VQT}.
FT   HELIX       257    259       {ECO:0000244|PDB:3VQT}.
FT   HELIX       263    273       {ECO:0000244|PDB:3VQT}.
FT   STRAND      280    287       {ECO:0000244|PDB:3VQT}.
FT   STRAND      295    302       {ECO:0000244|PDB:3VQT}.
FT   STRAND      313    321       {ECO:0000244|PDB:3VQT}.
FT   STRAND      328    331       {ECO:0000244|PDB:3VQT}.
FT   TURN        332    335       {ECO:0000244|PDB:3VQT}.
FT   STRAND      336    339       {ECO:0000244|PDB:3VQT}.
FT   STRAND      362    366       {ECO:0000244|PDB:3VQT}.
FT   STRAND      376    382       {ECO:0000244|PDB:3VQT}.
FT   STRAND      390    392       {ECO:0000244|PDB:3VQT}.
FT   STRAND      395    403       {ECO:0000244|PDB:3VQT}.
FT   HELIX       405    407       {ECO:0000244|PDB:3VQT}.
FT   HELIX       408    420       {ECO:0000244|PDB:3VQT}.
FT   STRAND      423    432       {ECO:0000244|PDB:3VQT}.
FT   STRAND      436    441       {ECO:0000244|PDB:3VQT}.
FT   HELIX       443    456       {ECO:0000244|PDB:3VQT}.
FT   STRAND      460    464       {ECO:0000244|PDB:3VQT}.
FT   STRAND      469    474       {ECO:0000244|PDB:3VQT}.
FT   HELIX       478    487       {ECO:0000244|PDB:3VQT}.
FT   HELIX       489    491       {ECO:0000244|PDB:3VQT}.
FT   STRAND      492    495       {ECO:0000244|PDB:3VQT}.
FT   STRAND      500    506       {ECO:0000244|PDB:3VQT}.
FT   HELIX       507    516       {ECO:0000244|PDB:3VQT}.
FT   STRAND      520    527       {ECO:0000244|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
//
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