P54263 (SYN_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	asparaginyl-tRNA aminoacylation Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Asparagine--tRNA ligase HAMAP-Rule MF_00534		PRO_0000176470
Experimental info
	Sequence conflict	355	1	A → R in CAA62491. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54263 [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] [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.
RefSeq	YP_143974.1. NC_006461.1.
3D structure databases
ProteinModelPortal	P54263.
ModBase	Search...
Protein-protein interaction databases
STRING	300852.TTHA0708.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAD70531; BAD70531; BAD70531.
GeneID	3168522.
KEGG	ttj:TTHA0708.
PATRIC	23956393. VBITheThe93045_0702.
Phylogenomic databases
eggNOG	COG0017.
HOGENOM	HOG000226034.
KO	K01893.
OMA	EFWHAEA.
ProtClustDB	PRK03932.
Enzyme and pathway databases
BRENDA	6.1.1.22. 6341.
Family and domain databases
Gene3D	2.40.50.140. 1 hit.
HAMAP	MF_00534. Asn_tRNA_synth.
InterPro	IPR004364. 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]
PANTHER	PTHR22594. PTHR22594. 1 hit. PTHR22594:SF6. PTHR22594:SF6. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
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:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program