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C1CV26 (SYN_DEIDV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. 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:Deide_11380
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length445 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 By similarity 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 – 445445Asparagine--tRNA ligase HAMAP MF_00534
PRO_1000211901

Sequences

Sequence LengthMass (Da)Tools
C1CV26 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 570586EDC6AE506E

FASTA44550,937
        10         20         30         40         50         60 
MISNIRDLKQ HVGETVTLQA WLTDKSGKGK IQFLKLRDGS GFVQATVFKN DVEEEVFESA 

        70         80         90        100        110        120 
KRLTQEQALT LTGEVRADER APGGVELSVR RLSPISENHA EYPITPKEHG IEFLMDQRHL 

       130        140        150        160        170        180 
WLRHRRPWAI MRIRDCVQRA IVDFFHSEGF VRFDAPFFTP NAAEGTTELF EIDLFGEDKA 

       190        200        210        220        230        240 
YLSQTGQLHA EAGAFAFGKV YTFGPTFRAE KSKTRRHLLE FWMVEPEVAP SNHKQNMDLQ 

       250        260        270        280        290        300 
ERFVSFLVRR ALDECTVELE MLGRDLSKLK GAAEGNYPRV TYTEALEIVR QHIENKDLPP 

       310        320        330        340        350        360 
NVQEDVQPVE WGDDLGAPHE TILGHHFDRP VMIEKYPAAI KAFYMQPDPE DSRVALCDDM 

       370        380        390        400        410        420 
IAPEGYGEII GGSERIHDYD LLKSRIEHEG LPLEAFDWYL DLRRVGSVPH AGFGMGLERV 

       430        440 
IAWISGIDHI REAIPFPRML TRMRP 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed: 19370165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001114 Genomic DNA. Translation: ACO46043.1.
RefSeqYP_002785797.1. NC_012526.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC1CV26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7738361.
GenomeReviewsGene locus Deide_11380 in contig CP001114_GR.
KEGGddr:Deide_11380.
PATRIC21616034. VBIDeiDes121019_1298.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMADHLPQET.
ProtClustDBPRK03932.

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_DEIDV
AccessionPrimary (citable) accession number: C1CV26
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: January 25, 2012
This is version 23 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