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O67589 (SYD_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. 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:
Aspartate--tRNA ligase

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:aspS
Ordered Locus Names:aq_1677
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044_B

Subunit structure

Homodimer By similarity. HAMAP MF_00044_B

Subcellular location

Cytoplasm HAMAP MF_00044_B.

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
Reference proteome
Gene Ontology (GO)
   Biological processtRNA aminoacylation for protein translation

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

aspartate-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 – 603603Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_0000110818

Sequences

Sequence LengthMass (Da)Tools
O67589 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9DFFBD840C8DCC1C

FASTA60369,729
        10         20         30         40         50         60 
MLTEYGDFKR TKYCGEVSEE DIGKEVKLAG WVHRKRHHGG VIFIDLRDRE GIVQVVVEEK 

        70         80         90        100        110        120 
TNPEAYEVAD KLKSEYVIGV VGKVRKRPEG TENPKLKTGY VEVVADRILV FNTSEALPFP 

       130        140        150        160        170        180 
VEEETHVSEE TKLKYRYIDL RRESMKNNLI FRHRVYQITR NFFTKEGFIE IETPFLTKST 

       190        200        210        220        230        240 
PEGARDFLVP SRLHPGKFYA LPQSPQLFKQ ILMIAGFDRY FQIVKCFRDE DLRADRQPEF 

       250        260        270        280        290        300 
TQIDYEMSFV SEEEVMDVAE RLIATLFKEL LGVELKTPFE RISYREAMEK YGTDKPDRRF 

       310        320        330        340        350        360 
GLELIELTDI FKNTAFKVFK SVVEAGGIIK AINFKGSNLS RKEIDELTKF VQSLGAKGLA 

       370        380        390        400        410        420 
WIKVEKDKLT SPIVKFFTEE ETQKLLERTK AEPGDVILFS ADKKEMVYKI LGNLRLHLGK 

       430        440        450        460        470        480 
KYKLIDESKW DVFWIVDFPL MEWDEEEERF VSLHHPFTMP REENIPKLKE ALEEEDLEKK 

       490        500        510        520        530        540 
KEIVHSVRAR AYDMVLNGEE IGGGSIRIHR RDIQEVVFKL LGIGEVEAQE KFGFLLEALK 

       550        560        570        580        590        600 
YGAPPHGGLA FGLDRVVALM LGLDSIRDTI AFPKTQRGIC PLTGAPDYVD PKQLKELHIK 


VLE 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07548.1.
PIRD70445.
RefSeqNP_214155.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67589.
SMRO67589. Positions 8-602.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193305.
GenomeReviewsGene locus aq_1677 in contig AE000657_GR.
KEGGaae:aq_1677.
NMPDRfig|224324.1.peg.1170.
PATRIC20960370. VBIAquAeo85532_1296.

Phylogenomic databases

HOGENOMHBG396032.
OMAAFPKTQQ.
PhylomeDBO67589.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1677-MONOMER.

Family and domain databases

HAMAPMF_00044_B. Asp_tRNA_synth_B.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01876.
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.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. AspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_AQUAE
AccessionPrimary (citable) accession number: O67589
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 86 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