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UniProtKB/Swiss-Prot entry P00952

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SYY_BACST
Primary accession number P00952
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 78)
Name and origin of the protein
Protein name Tyrosyl-tRNA synthetase
Synonyms EC 6.1.1.1
Tyrosine--tRNA ligase
TyrRS
Gene name
Name: tyrS
From
Bacillus stearothermophilus (Geobacillus stearothermophilus) [TaxID: 1422] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6840095 [NCBI, ExPASy, EBI, Israel, Japan]
Winter G., Koch G.L.E., Hartley B.S., Barker D.G.;
"The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus.";
Eur. J. Biochem. 132:383-387(1983).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=3525162 [NCBI, ExPASy, EBI, Israel, Japan]
Waye M.M.Y., Winter G.;
"A transcription terminator in the 5' non-coding region of the tyrosyl tRNA synthetase gene from Bacillus stearothermophilus.";
Eur. J. Biochem. 158:505-510(1986).
[3]
 BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=6315404 [NCBI, ExPASy, EBI, Israel, Japan]
Waye M.M.Y., Winter G., Wilkinson A.J., Fersht A.R.;
"Deletion mutagenesis using an 'M13 splint': the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate.";
EMBO J. 2:1827-1829(1983).
[4]
 INTERACTION WITH TRNA(TYR).
PubMed=3006039 [NCBI, ExPASy, EBI, Israel, Japan]
Carter P., Bedouelle H., Winter G.;
"Construction of heterodimer tyrosyl-tRNA synthetase shows tRNATyr interacts with both subunits.";
Proc. Natl. Acad. Sci. U.S.A. 83:1189-1192(1986).
[5]
 MUTAGENESIS OF HIS-45; GLU-152; THR-224; LYS-410 AND LYS-411.
DOI=10.1016/0022-2836(92)90991-R; PubMed=1542120 [NCBI, ExPASy, EBI, Israel, Japan]
Vidal-Cros A., Bedouelle H.;
"Role of residue Glu152 in the discrimination between transfer RNAs by tyrosyl-tRNA synthetase from Bacillus stearothermophilus.";
J. Mol. Biol. 223:801-810(1992).
[6]
 MUTAGENESIS OF LYS-230; PHE-231; GLY-232; LYS-233 AND THR-234.
DOI=10.1021/bi991675l; PubMed=10630994 [NCBI, ExPASy, EBI, Israel, Japan]
Xin Y., Li W., First E.A.;
"The 'KMSKS' motif in tyrosyl-tRNA synthetase participates in the initial binding of tRNA(Tyr).";
Biochemistry 39:340-347(2000).
[7]
 MUTAGENESIS OF THR-40; HIS-45; HIS-48; LYS-82 AND ARG-86.
DOI=10.1006/jmbi.2000.4125; PubMed=11023793 [NCBI, ExPASy, EBI, Israel, Japan]
Xin Y., Li W., Dwyer D.S., First E.A.;
"Correlating amino acid conservation with function in tyrosyl-tRNA synthetase.";
J. Mol. Biol. 303:287-298(2000).
[8]
 MUTAGENESIS OF ASP-78; TYR-169; GLN-173; ASP-194 AND GLN-195.
DOI=10.1006/jmbi.2000.4126; PubMed=11023794 [NCBI, ExPASy, EBI, Israel, Japan]
Xin Y., Li W., First E.A.;
"Stabilization of the transition state for the transfer of tyrosine to tRNA(Tyr) by tyrosyl-tRNA synthetase.";
J. Mol. Biol. 303:299-310(2000).
[9]
 MUTAGENESIS OF LEU-322; PHE-323; SER-324; GLY-325 AND PHE-339.
DOI=10.1021/bi010208c; PubMed=11401566 [NCBI, ExPASy, EBI, Israel, Japan]
Gaillard C., Bedouelle H.;
"An essential residue in the flexible peptide linking the two idiosynchratic domains of bacterial tyrosyl-tRNA synthetases.";
Biochemistry 40:7192-7199(2001).
[10]
 X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1016/0022-2836(82)90255-8; PubMed=7120416 [NCBI, ExPASy, EBI, Israel, Japan]
Bhat T.N., Blow D.M., Brick P., Nyborg J.;
"Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.";
J. Mol. Biol. 158:699-709(1982).
[11]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/0022-2836(89)90090-9; PubMed=2504923 [NCBI, ExPASy, EBI, Israel, Japan]
Brick P., Bhat T.N., Blow D.M.;
"Structure of tyrosyl-tRNA synthetase refined at 2.3-A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate.";
J. Mol. Biol. 208:83-98(1989).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J01546; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X04193; CAA27784.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01179; SYBSYF.
3D structure databases
PDB
1JH3; NMR; -; A=321-419.[ExPASy / RCSB / EBI]
1TYA; X-ray; 2.80 A; E=1-319.[ExPASy / RCSB / EBI]
1TYB; X-ray; 2.50 A; E=1-319.[ExPASy / RCSB / EBI]
1TYC; X-ray; 2.50 A; A=1-319.[ExPASy / RCSB / EBI]
1TYD; X-ray; 2.50 A; E=1-319.[ExPASy / RCSB / EBI]
2TS1; X-ray; 2.30 A; A=1-419.[ExPASy / RCSB / EBI]
3TS1; X-ray; 2.70 A; A=1-419.[ExPASy / RCSB / EBI]
4TS1; X-ray; 2.50 A; A/B=1-317.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JH3; -.
1TYA; -.
1TYB; -.
1TYC; -.
1TYD; -.
2TS1; -.
3TS1; -.
4TS1; -.
DisProt DP00095; -.
ModBase P00952.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0004831; Molecular function: tyrosine-tRNA ligase activity (inferred from electronic annotation from HAMAP).
GO:0006437; Biological process: tyrosyl-tRNA aminoacylation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_02006; -; 1.
PBIL [Tree]
InterPro IPR001412; aa-tRNA-synth_I_CS.
IPR002305; aa-tRNA-synth_Ib.
IPR014729; Rossmann-like_a/b/a_fold.
IPR002942; S4_RNA_bd.
IPR002307; Tyr-tRNA-synth_Ib_bac/mito.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
PANTHER PTHR11766; Tyr_tRNA-synt_1b; 1.
Pfam PF01479; S4; 1.
PF00579; tRNA-synt_1b; 1.
Pfam graphical view of domain structure.
PRINTS PR01040; TRNASYNTHTYR.
SMART SM00363; S4; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00234; tyrS; 1.
PROSITE PS00178; AA_TRNA_LIGASE_I; 1.
PS50889; S4; 1.
PROSITE graphical view of domain structure (profiles).
Other
LinkHub P00952; -.
ProtoNet P00952.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   419  419     Tyrosyl-tRNA synthetase. PRO_0000055642
DOMAIN   352   419  68     S4 RNA-binding. 
MOTIF   39    48  10     "HIGH" region. 
MOTIF   230   234  5     "KMSKS" region. 
BINDING   34    34        Tyrosine (By similarity). 
BINDING   169   169        Tyrosine (By similarity). 
BINDING   173   173        Tyrosine (By similarity). 
BINDING   233   233        ATP (By similarity). 
MUTAGEN   40    40        T->A: Destabilizes the transition states for both steps of the reaction. 
MUTAGEN   45    45        H->A: Does not affect the second step of the reaction. 
MUTAGEN   45    45        H->N: Decreases the rate of formation of Tyr-AMP and, as a consequence, abolishes the aminoacylation activity. Strongly increases the toxicity; when associated with A-152. 
MUTAGEN   48    48        H->A: Does not affect the second step of the reaction. 
MUTAGEN   78    78        D->A: Does not affect the initial binding of tRNA(Tyr) and the stability of the transition state for the second step of the reaction. 
MUTAGEN   82    82        K->A: Destabilizes the transition states for both steps of the reaction. 
MUTAGEN   86    86        R->A: Destabilizes the transition states for both steps of the reaction. 
MUTAGEN   152   152        E->A: Mischarges tRNA(Phe) with tyrosine in vitro. Toxic for the cell, probably because it alters the discrimination of TyrRS against non-cognate tRNAs. The toxicity is abolished; when associated with N-410 or N-411. Strongly increases toxicity; when associated with N-45. Enhances the toxicity; when associated with A-224. 
MUTAGEN   152   152        E->D: Does not charge tRNA(Phe) in vitro with tyrosine. 
MUTAGEN   152   152        E->Q: Mischarges tRNA(Phe) with tyrosine in vitro but this mutation is not toxic in vivo. 
MUTAGEN   169   169        Y->A: Does not affect the initial binding of tRNA(Tyr) and the stability of the transition state for the second step of the reaction. 
MUTAGEN   173   173        Q->A: Destabilizes the transition state for the second step of the reaction. 
MUTAGEN   194   194        D->A: Destabilizes the transition state for the first step of the reaction, but does not affect the transition state for the second step. 
MUTAGEN   195   195        Q->A: Destabilizes the transition state for the first step of the reaction, but does not affect the transition state for the second step. 
MUTAGEN   224   224        T->A: Is not toxic in itself. Enhances the toxicity; when associated with A-152. 
MUTAGEN   230   230        K->A: Decreases the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 
MUTAGEN   231   231        F->L: No effect on the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 
MUTAGEN   232   232        G->A: No effect on the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 
MUTAGEN   233   233        K->A: Decreases the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 
MUTAGEN   234   234        T->A: No effect on the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 
MUTAGEN   322   322        L->P: 50-fold decrease in charging of tRNA(Tyr) with tyrosine. 
MUTAGEN   323   323        F->A: 90-fold decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 
MUTAGEN   323   323        F->L: 67-fold decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 
MUTAGEN   323   323        F->W: Weak decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 
MUTAGEN   323   323        F->Y: 3-fold decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 
MUTAGEN   324   324        S->A: 2-fold increase in charging of tRNA(Tyr) with tyrosine. 
MUTAGEN   325   325        G->A: 5-fold increase in charging of tRNA(Tyr) with tyrosine. 
MUTAGEN   339   339        F->L: Has no effect on charging of tRNA(Tyr) with tyrosine. 
MUTAGEN   410   410        K->N: Decreases the binding of tRNA(Tyr), without affecting the formation of Tyr-AMP. Abolishes the toxicity; when associated with A-152. 
MUTAGEN   411   411        K->N: Decreases the binding of tRNA(Tyr), without affecting the formation of Tyr-AMP. Abolishes the toxicity; when associated with A-152. 
HELIX   2    10  9      
STRAND   14    17  4      
HELIX   19    28  10      
STRAND   32    37  6      
STRAND   40    43  4      
HELIX   46    48  3      
HELIX   49    60  12      
STRAND   64    69  6      
HELIX   73    75  3      
HELIX   91   105  15      
STRAND   114   116  3      
STRAND   119   122  4      
HELIX   124   127  4      
HELIX   132   138  7      
HELIX   140   142  3      
HELIX   145   149  5      
HELIX   152   155  4      
TURN   156   160  5      
HELIX   164   184  21      
STRAND   186   192  7      
HELIX   193   195  3      
HELIX   196   210  15      
STRAND   216   220  5      
STRAND   240   242  3      
TURN   243   245  3      
HELIX   248   256  9      
HELIX   260   270  11      
HELIX   275   287  13      
HELIX   293   307  15      
HELIX   309   318  10      
STRAND   325   327  3      
HELIX   332   339  8      
STRAND   344   347  4      
HELIX   354   361  8      
HELIX   367   375  9      
STRAND   379   381  3      
TURN   389   391  3      
TURN   396   398  3      
STRAND   399   408  10      
STRAND   413   418  6      
Sequence information
Length: 419 AA [This is the length of the unprocessed precursor] Molecular weight: 47303 Da [This is the MW of the unprocessed precursor] CRC64: B9CB64AEEEE2010F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDLLAELQWR GLVNQTTDED GLRKLLNEER VTLYCGFDPT ADSLHIGHLA TILTMRRFQQ 

        70         80         90        100        110        120 
AGHRPIALVG GATGLIGDPS GKKSERTLNA KETVEAWSAR IKEQLGRFLD FEADGNPAKI 

       130        140        150        160        170        180 
KNNYDWIGPL DVITFLRDVG KHFSVNYMMA KESVQSRIET GISFTEFSYM MLQAYDFLRL 

       190        200        210        220        230        240 
YETEGCRLQI GGSDQWGNIT AGLELIRKTK GEARAFGLTI PLVTKADGTK FGKTESGTIW 

       250        260        270        280        290        300 
LDKEKTSPYE FYQFWINTDD RDVIRYLKYF TFLSKEEIEA LEQELREAPE KRAAQKTLAE 

       310        320        330        340        350        360 
EVTKLVHGEE ALRQAIRISE ALFSGDIANL TAAEIEQGFK DVPSFVHEGG DVPLVELLVS 

       370        380        390        400        410 
AGISPSKRQA REDIQNGAIY VNGERLQDVG AILTAEHRLE GRFTVIRRGK KKYYLIRYA
P00952 in FASTA format

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View entry in raw text format (no links)
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