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Q8A0Z8 (SYN_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. 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:BT_3873
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_00534

Subcellular location

Cytoplasm HAMAP 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 electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Asparagine--tRNA ligase HAMAP MF_00534
PRO_0000176394

Sequences

Sequence LengthMass (Da)Tools
Q8A0Z8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4D3F1E9594A5F2EC

FASTA46753,295
        10         20         30         40         50         60 
MEKIGRTKIV DLLKREDIGA MVNVKGWVRT RRGSKQVNFI ALNDGSTINN VQIVVDLANF 

        70         80         90        100        110        120 
DEEMLKLITT GACISVNGVM VESVGSGQKV EVQAKEIEVL GTCDNTYPLQ KKGHSMEFLR 

       130        140        150        160        170        180 
EIAHLRPRTN TFGAVFRIRH NMAIAIHKFF HEKGFFYFHT PIITGSDCEG AGQMFQVTTM 

       190        200        210        220        230        240 
NLYDLKKDER GSISYDDDFF GKQASLTVSG QLEGELAATA LGAIYTFGPT FRAENSNTPR 

       250        260        270        280        290        300 
HLAEFWMIEP EVAFNDIADN MDLAEEFIKY CVKWALDNCA DDVKFLNDMF DKGLIERLQG 

       310        320        330        340        350        360 
VLKDDFVRLP YTDGIKILED AVAKGHKFEF PVYWGVDLAS EHERYLVEEH FKRPVILTDY 

       370        380        390        400        410        420 
PKEIKAFYMK QNEDGKTVRA MDVLFPKIGE IIGGSEREAD YNKLMTRIEE MHIPMKDMWW 

       430        440        450        460 
YLDTRKFGTC PHSGFGLGFE RLLLFVTGMS NIRDVIPFPR TPRNADF 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO78978.1.
RefSeqNP_812784.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A0Z8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1072981.
GenomeReviewsGene locus BT_3873 in contig AE015928_GR.
KEGGbth:BT_3873.
NMPDRfig|226186.1.peg.3871.
PATRIC21062776. VBIBacThe70966_3937.

Phylogenomic databases

HOGENOMHBG745843.
OMAAIHRFFH.
PhylomeDBQ8A0Z8.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycBTHE226186:BT_3873-MONOMER.

Family and domain databases

HAMAPMF_00534. Asn_tRNA_synth.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01893.
PANTHERPTHR22594. aa-tRNA-synt_II. 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_BACTN
AccessionPrimary (citable) accession number: Q8A0Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 62 of the entry and version 1 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