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Reviewed, UniProtKB/Swiss-Prot A7ZK21 (SYN_ECO24)

Last modified February 9, 2010. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: EcE24377A_1030
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Asparaginyl-tRNA synthetase HAMAP MF_00534
PRO_1000061018

Sequences

Sequence LengthMass (Da)Tools
A7ZK21-1 [UniParc].

Last modified October 23, 2007. 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]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV18888.1.
RefSeqYP_001462150.1.

3D structure databases

SMRA7ZK21. Positions 16-464.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZK21.

Genome annotation databases

GeneID5587779.
GenomeReviewsGene locus EcE24377A_1030 in contig CP000800_GR.
KEGGecw:EcE24377A_1030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHBG745843.
OMALQKKRHS.

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_cons-dom.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp-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.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00457. asnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYN_ECO24
AccessionPrimary (citable) accession number: A7ZK21
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: February 9, 2010
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents