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Q1RDS7 (SYN_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:UTI89_C1002
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length466 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
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 – 466466Asparagine--tRNA ligase HAMAP MF_00534
PRO_1000051393

Sequences

Sequence LengthMass (Da)Tools
Q1RDS7 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 1E477CB5467B772F

FASTA46652,570
        10         20         30         40         50         60 
MSVVPVADVL QGRVAVDSEV TVRGWVRTRR DSKAGISFLA VYDGSCFDPV QAVINNSLPN 

        70         80         90        100        110        120 
YNEDVLRLTT GCSVIVTGKV VASPGQGQQF EIQASKVEVA GWVEDPDTYP MAAKRHSIEY 

       130        140        150        160        170        180 
LREVAHLRPR TNLIGAVARV RHTLAQALHR FFNEQGFFWV STPLITASDT EGAGEMFRVS 

       190        200        210        220        230        240 
TLDLENLPRN DQGKVDFDKD FFGKESFLTV SGQLNGETYA CALSKIYTFG PTFRAENSNT 

       250        260        270        280        290        300 
SRHLAEFWML EPEVAFANLN DIAGLAEAML KYVFKAVLEE RADDMKFFAE RVDKDAVSRL 

       310        320        330        340        350        360 
ERFIEADFAQ VDYTDAVTIL ENCGRKFENP VYWGVDLSSE HERYLAEEHF KAPVVVKNYP 

       370        380        390        400        410        420 
KDIKAFYMRL NEDGKTVAAM DVLAPGIGEI IGGSQREERL DVLDERMLEM GLNKEDYWWY 

       430        440        450        460 
RDLRRYGTVP HSGFGLGFER LIAYVTGVQN VRDVIPFPRT PRNASF 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000243 Genomic DNA. Translation: ABE06487.1.
RefSeqYP_540018.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1RDS7.
SMRQ1RDS7. Positions 6-465.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1RDS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000068038; EBESCP00000065516; EBESCG00000067085.
GeneID3992829.
GenomeReviewsGene locus UTI89_C1002 in contig CP000243_GR.
KEGGeci:UTI89_C1002.
PATRIC18451645. VBIEscCol42261_1078.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0017.
GeneTreeEBGT00050000009271.
HOGENOMHBG745843.
OMAAIHRFFH.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C1002-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_ECOUT
AccessionPrimary (citable) accession number: Q1RDS7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 49 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