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Reviewed, UniProtKB/Swiss-Prot P54263 (SYN_THET8)

Last modified November 3, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Asparaginyl-tRNA synthetase
    EC=6.1.1.22
Alternative name(s):
    Asparagine--tRNA ligase
      Short name=AsnRS
Gene names
Name: asnS
Ordered Locus Names: TTHA0708
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). HAMAP MF_00534

Subunit structure

Homodimer. HAMAP MF_00534

Subcellular location

Cytoplasm. HAMAP MF_00534

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Asparaginyl-tRNA synthetase HAMAP MF_00534
PRO_0000176470

Experimental info

Sequence conflict3551A → R in CAA62491. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54263-1 [UniParc].

Last modified May 24, 2005. Version 2.
Checksum: B6A22A7D08F3D496

FASTA43850,785
        10         20         30         40         50         60 
MRVFIDEIAR HVDQEVELRG WLYQRRSKGK IHFLILRDGT GFLQATVVQG EVPEAVFREA 

        70         80         90        100        110        120 
DHLPQETALR VWGRVREDRR APGGFELAVR DLQVVSRPQG EYPIGPKEHG IDFLMDHRHL 

       130        140        150        160        170        180 
WLRHRRPFAV MRIRDELERA IHEFFGERGF LRFDAPILTP SAVEGTTELF EVELFDGEKA 

       190        200        210        220        230        240 
YLSQSGQLYA EAGALAFAKV YTFGPTFRAE RSKTRRHLLE FWMVEPEVAF MTHEENMALQ 

       250        260        270        280        290        300 
EELVSFLVAR VLERRSRELE MLGRDPKALE PAAEGHYPRL TYKEAVALVN RIAQEDPEVP 

       310        320        330        340        350        360 
PLPYGEDFGA PHEAALSRRF DRPVFVERYP ARIKAFYMEP DPEDPELVLN DDLLAPEGYG 

       370        380        390        400        410        420 
EIIGGSQRIH DLELLRRKIQ EFGLPEEVYD WYLDLRRFGS VPHSGFGLGL ERTVAWICGL 

       430 
AHVREAIPFP RMYTRMRP 

« Hide

References

« Hide 'large scale' references
[1]"Asparaginyl-tRNA synthetase from Thermus thermophilus HB8. Sequence of the gene and crystallization of the enzyme expressed in Escherichia coli."
Seignovert L., Haertlein M., Leberman R.
Eur. J. Biochem. 239:501-508(1996) [PubMed: 8706760] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CRYSTALLIZATION.
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid."
Berthet-Colominas C., Seignovert L., Haertlein M., Grotli M., Cusack S., Leberman R.
EMBO J. 17:2947-2960(1998) [PubMed: 9582288] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

X91009 Genomic DNA. Translation: CAA62491.1.
AP008226 Genomic DNA. Translation: BAD70531.1.
RefSeqYP_143974.1.

3D structure databases

HSSPHSSP built from PDB template 1N9W based on UniProtKB Q9LCY8.
ModBaseSearch...

Protein-protein interaction databases

STRINGP54263.

Genome annotation databases

GeneID3168522.
GenomeReviewsGene locus TTHA0708 in contig AP008226_GR.
KEGGttj:TTHA0708.
NMPDRfig|300852.3.peg.713.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP54263.
OMALQKKRHS.

Enzyme and pathway databases

BioCycTTHE300852:TTHA0708-MON.
BRENDA6.1.1.22. 245.

Family and domain databases

HAMAPMF_00534.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp-tRNA-synth_IIb.
IPR004365. NA_bd_OB_tRNA-helicase.
[Graphical view]
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00457. asnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYN_THET8
AccessionPrimary (citable) accession number: P54263
Secondary accession number(s): Q5SKD5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 24, 2005
Last modified: November 3, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

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