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Q1IZA1 (SYN_DEIGD) 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:Dgeo_1136
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length449 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 – 449449Asparagine--tRNA ligase HAMAP MF_00534
PRO_1000081847

Sequences

Sequence LengthMass (Da)Tools
Q1IZA1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 2886179F29A6AFF2

FASTA44950,633
        10         20         30         40         50         60 
MTVIPNVSID ALKNHVGETV RVNAWLTDKS GKGKLQFLKL RDGSGFVQAT VFKGDVPEEV 

        70         80         90        100        110        120 
FEAARRLSQE QAVRVTGEVR ADERAPGGVE LAVRDLVPFA ANQAEYPITP KEHGIEFLLD 

       130        140        150        160        170        180 
HRHLWLRHRR PWAILRVRDC VERAIVEFFH QEGFIRFDAP FFTPNAAEGT TELFEIDLFG 

       190        200        210        220        230        240 
EDKAYLSQTG QLHAEAGALA FGKVYTFGPT FRAEKSKTRR HLLEFWMVEP EVAPATHQDN 

       250        260        270        280        290        300 
MDLQERLVSF LVRRVLEECA AELAVLGRDV AKLQPAAEGN YPRVTYTEAL DIIRRHIAEG 

       310        320        330        340        350        360 
DLPPNVQPDV QPVEWGDDLG APHETILGFH FDRPVIVERY PAAIKAFYMQ PDPADPRLAL 

       370        380        390        400        410        420 
CDDMIAPEGY GEIIGGSERI HDYTLLKARI EGEGLPLSAF DWYLDLRRFG SVPHAGFGMG 

       430        440 
LERVIAWITG IDHIREAIPF PRMLTRMVP 

« Hide

References

[1]"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000359 Genomic DNA. Translation: ABF45433.1.
RefSeqYP_604602.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IZA1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1IZA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4058304.
GenomeReviewsGene locus Dgeo_1136 in contig CP000359_GR.
KEGGdge:Dgeo_1136.
NMPDRfig|68909.1.peg.2106.
PATRIC21624157. VBIDeiGeo41128_1715.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHBG745843.
OMADHLPQET.
PhylomeDBQ1IZA1.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycDGEO319795:DGEO_1136-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_DEIGD
AccessionPrimary (citable) accession number: Q1IZA1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 13, 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