Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A0JXA1 (SYD_ARTS2)

Last modified June 16, 2009. Version 22. 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:
    Aspartyl-tRNA synthetase
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
Gene names
Name: aspS
Ordered Locus Names: Arth_2291
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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 processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 596596Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_1000006633

Sequences

Sequence LengthMass (Da)Tools
A0JXA1-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: C92073621960756E

FASTA59665,331
        10         20         30         40         50         60 
MLRTHDLGSL RSEHIGQTVT LAGWVGRRRD HGGVAFVDLR DASGVSQVVV REEEVFHGLR 

        70         80         90        100        110        120 
NEYVLQVIGT VSQRPEGNEN PALATGQIEV IAEKVTILNT SDPLPFQIDE HVEVGEEARL 

       130        140        150        160        170        180 
KHRYLDLRRP GPARNMRLRS EANRVARELL HRDGYVEIET PTLTRSTPEG ARDFVVPARL 

       190        200        210        220        230        240 
APGSWYALPQ SPQLFKQLLQ VGGFEKYYQI ARCYRDEDFR ADRQPEFTQL DIEASFVEQD 

       250        260        270        280        290        300 
DIISLGESIV KALWQLIDVE IPTPIQRITY ADAMARYGSD KPDLRFGLEL TELTEFFKDT 

       310        320        330        340        350        360 
NFGVFKAPYV GAVVMPGGAS QARRALDAWQ EWAKQRGAKG LAYVLFKEDG ELAGPVAKNL 

       370        380        390        400        410        420 
TDTERAGLAD AVGAKPGDCI FFAAGEKTPS RALLGAARVE IGHRTGLINP ADWAFCWVVD 

       430        440        450        460        470        480 
APMFEPAAAA VASGDVAVGA GQWTAVHHAF TSPKPEFMDS FDKDPESALS YAYDIVCNGN 

       490        500        510        520        530        540 
EIGGGSIRIH ERDVQERVFE LMGLDKADAE TKFGFLLEGF KFGAPPHGGI AFGWDRVVAL 

       550        560        570        580        590 
LAGVESIRDV IAFPKSGGGY DPLTQAPAPI TAQQRKEAGV DFKPEAKKAD PGATKA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000454 Genomic DNA. Translation: ABK03671.1.
RefSeqYP_831771.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4445334.
GenomeReviewsGene locus Arth_2291 in contig CP000454_GR.
KEGGart:Arth_2291.
TIGRArth_2291.

Phylogenomic databases

OMAA0JXA1. VDRRRDH.

Family and domain databases

HAMAPMF_00044.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002312. Asp-tRNA-synth_IIb.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR004115. GAD.
IPR004365. NA_bd_OB_tRNA-helicase.
[Graphical view]
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF5. AspS_bac. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_ARTS2
AccessionPrimary (citable) accession number: A0JXA1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: June 16, 2009
This is version 22 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