[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION. DOI=10.1111/j.1432-1033.1996.0501u.x; PubMed=8706760 [NCBI, ExPASy, EBI, Israel, Japan] Seignovert L., Haertlein M., Leberman R.; "Asparaginyl-tRNA synthetase from Thermus thermophilus HB8. Sequence of the gene and crystallization of the enzyme expressed in Escherichia coli."; Eur. J. Biochem. 239:501-508(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; "Complete genome sequence of Thermus thermophilus HB8."; Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[3]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1093/emboj/17.10.2947; PubMed=9582288 [NCBI, ExPASy, EBI, Israel, Japan] Berthet-Colominas C., Seignovert L., Haertlein M., Grotli M., Cusack S., Leberman R.; "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."; EMBO J. 17:2947-2960(1998).

Comments

CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family [view classification].

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

X91009; CAA62491.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008226; BAD70531.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_143974.1; -.

3D structure databases

HSSP

Q9LCY8; 1N9W. [HSSP ENTRY / PDB]

ModBase

P54263.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0708-MON; -.

BRENDA

6.1.1.22; 245.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0004816;	Molecular function: asparagine-tRNA ligase activity (inferred from direct assay from UniProtKB).
GO:0004815;	Molecular function: aspartate-tRNA ligase activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003676;	Molecular function: nucleic acid binding (inferred from electronic annotation from InterPro).
GO:0006421;	Biological process: asparaginyl-tRNA aminoacylation (inferred from electronic annotation from HAMAP).
GO:0006422;	Biological process: aspartyl-tRNA aminoacylation (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

HAMAP

MF_00534; -; 1.
PBIL [Tree]

InterPro

IPR004364; 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 of domain structure.

PANTHER

PTHR22594; aa-tRNA-synt_II; 1.

Pfam

PF00152; tRNA-synt_2; 1.
PF01336; tRNA_anti; 1.
Pfam graphical view of domain structure.

PRINTS

PR01042; TRNASYNTHASP.

TIGRFAMs

TIGR00457; asnS; 1.

PROSITE

PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

3168522; -.

GenomeReviews

AP008226_GR; TTHA0708.

KEGG

ttj:TTHA0708; -.

NMPDR

fig|300852.3.peg.713; -.

Phylogenomic databases

HOGENOM

P54263; -.

OMA

P54263; LQKKRHS.

Genome annotation databases

CMR

P54263; TTHA0708.

Other

ProtoNet

P54263.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 438`	`438`	`Asparaginyl-tRNA synthetase.`	`PRO_0000176470`
`CONFLICT`	`355 355`		`A -> R (in Ref. 1; CAA62491).`

Sequence information

Length: 438 AA [This is the length of the unprocessed precursor]

Molecular weight: 50785 Da [This is the MW of the unprocessed precursor]

CRC64: B6A22A7D08F3D496 [This is a checksum on the sequence]

        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

P54263 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools