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Reviewed, UniProtKB/Swiss-Prot P36419 (SYD_THETH)

Last modified February 9, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Aspartyl-tRNA synthetase
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
Gene names
Name: aspS
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044

Subunit structure

Homodimer. HAMAP MF_00044

Subcellular location

Cytoplasm HAMAP MF_00044.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_0000110971

Secondary structure

1 ..................................................................................................... 580
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P36419-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 510C79B25CF95D4E

FASTA58066,030
        10         20         30         40         50         60 
MRRTHYAGSL RETHVGEEVV LEGWVNRRRD LGGLIFLDLR DREGLVQLVA HPASPAYATA 

        70         80         90        100        110        120 
ERVRPEWVVR AKGLVRLRPE PNPRLATGRV EVELSALEVL AEAKTPPFPV DAGWRGEEEK 

       130        140        150        160        170        180 
EASEELRLKY RYLDLRRRRM QENLRLRHRV IKAIWDFLDR EGFVQVETPF LTKSTPEGAR 

       190        200        210        220        230        240 
DFLVPYRHEP GLFYALPQSP QLFKQMLMVA GLDRYFQIAR CFRDEDLRAD RQPDFTQLDL 

       250        260        270        280        290        300 
EMSFVEVEDV LELNERLMAH VFREALGVEL PLPFPRLSYE EAMERYGSDK PDLRFGLELK 

       310        320        330        340        350        360 
EVGPLFRQSG FRVFQEAESV KALALPKALS RKEVAELEEV AKRHKAQGLA WARVEEGGFS 

       370        380        390        400        410        420 
GGVAKFLEPV REALLQATEA RPGDTLLFVA GPRKVAATAL GAVRLRAADL LGLKREGFRF 

       430        440        450        460        470        480 
LWVVDFPLLE WDEEEEAWTY MHHPFTSPHP EDLPLLEKDP GRVRALAYDL VLNGVEVGGG 

       490        500        510        520        530        540 
SIRIHDPRLQ ARVFRLLGIG EEEQREKFGF FLEALEYGAP PHGGIAWGLD RLLALMTGSP 

       550        560        570        580 
SIREVIAFPK NKEGKDPLTG APSPVPEEQL RELGLMVVRP

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References

[1]"Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases."
Poterszman A., Plateau P., Moras D., Blanquet S., Mazuric M.-H., Kreutzer R., Kern D.
FEBS Lett. 325:183-186(1993) [PubMed: 8319804] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: VK1.
[2]"Crystal structure of a prokaryotic aspartyl tRNA-synthetase."
Delarue M., Poterszman A., Nikonov S., Garber M., Moras D., Thierry J.-C.
EMBO J. 13:3219-3229(1994) [PubMed: 8045252] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[3]"An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase."
Briand C., Poterszman A., Eiler S., Webster G., Thierry J.-C., Moras D.
J. Mol. Biol. 299:1051-1060(2000) [PubMed: 10843857] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X70943 Genomic DNA. Translation: CAA50282.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFWX-ray3.00A/B1-580[»]
1G51X-ray2.40A/B1-580[»]
1L0WX-ray2.01A/B1-580[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA6.1.1.12. 245.

Family and domain databases

HAMAPMF_00044_B. Asp_tRNA_synth_B.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR002312. Asp-tRNA-synth_IIb.
IPR020564. Asp-tRNA-synth_IIb_bac-type.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA_bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF5. AspS_bac. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.

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Entry information

Entry nameSYD_THETH
AccessionPrimary (citable) accession number: P36419
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 9, 2010
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents