Reviewed, UniProtKB/Swiss-Prot P54263 (SYN_THET8)

Names and origin

Protein names

Recommended 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

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP aspartyl-tRNA aminoacylation Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP asparagine-tRNA ligase activity Ref.1 Inferred from direct assay. Source: UniProtKB aspartate-tRNA ligase activity Inferred from electronic annotation. Source: InterPro nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Asparaginyl-tRNA synthetase HAMAP MF_00534		PRO_0000176470
Experimental info
	Sequence conflict	355	1	A → R in CAA62491. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54263-1 [UniParc]. Last modified May 24, 2005. Version 2. Checksum: B6A22A7D08F3D496	FASTA	438	50,785
	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

References

	« Hide 'large scale' referencesShow '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
EMBLGenBankDDBJ	X91009 Genomic DNA. Translation: CAA62491.1. AP008226 Genomic DNA. Translation: BAD70531.1.
RefSeq	YP_143974.1.
3D structure databases
HSSP	HSSP built from PDB template 1N9W based on UniProtKB Q9LCY8.
ModBase	Search...
Protein-protein interaction databases
STRING	P54263.
Genome annotation databases
GeneID	3168522.
GenomeReviews	Gene locus TTHA0708 in contig AP008226_GR.
KEGG	ttj:TTHA0708.
NMPDR	fig|300852.3.peg.713.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P54263.
OMA	LQKKRHS.
Enzyme and pathway databases
BioCyc	TTHE300852:TTHA0708-MON.
BRENDA	6.1.1.22. 245.
Family and domain databases
HAMAP	MF_00534. [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]
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00457. asnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYN_THET8

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)