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P54263 (SYN_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine--tRNA ligase

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

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00534.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processasparaginyl-tRNA aminoacylation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

asparagine-tRNA ligase activity

Inferred from direct assay Ref.1. Source: UniProtKB

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Asparagine--tRNA ligase HAMAP-Rule MF_00534
PRO_0000176470

Experimental info

Sequence conflict3551A → R in CAA62491. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54263 [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] [Europe PMC] [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].
Strain: HB8 / ATCC 27634 / DSM 579.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91009 Genomic DNA. Translation: CAA62491.1.
AP008226 Genomic DNA. Translation: BAD70531.1.
RefSeqYP_143974.1. NC_006461.1.

3D structure databases

ProteinModelPortalP54263.
ModBaseSearch...

Protein-protein interaction databases

STRING300852.TTHA0708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70531; BAD70531; BAD70531.
GeneID3168522.
KEGGttj:TTHA0708.
PATRIC23956393. VBITheThe93045_0702.

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHOG000226034.
KOK01893.
OMAEFWHAEA.
ProtClustDBPRK03932.

Enzyme and pathway databases

BRENDA6.1.1.22. 6341.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00534. Asn_tRNA_synth.
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004522. Asn-tRNA-ligase_IIb.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF6. PTHR22594:SF6. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
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: May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families