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Reviewed, UniProtKB/Swiss-Prot A6VQA9 (SYD_ACTSZ)

Last modified November 3, 2009. Version 18. 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: Asuc_1805
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length589 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 – 589589Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_1000071082

Sequences

Sequence LengthMass (Da)Tools
A6VQA9-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: B836012E164F3E56

FASTA58966,297
        10         20         30         40         50         60 
MMRSHYCGAL NRGNIGQEVT LSGWVHRRRD LGGLIFIDMR DREGIVQVCF DPKYQEALTA 

        70         80         90        100        110        120 
AADLRNEFCI QIKGEVTARP GNQINKNMAT GEVEVLAKAL SVYNASDVLP LDFNQNNTEE 

       130        140        150        160        170        180 
QRLKYRYLDL RRPEMAQRLK TRAKITSFVR RFMDDHGFLD IETPMLTKAT PEGARDYLVP 

       190        200        210        220        230        240 
SRVHKGKFYA LPQSPQLFKQ LLMMSGFDRY YQIVKCFRDE DLRADRQPEF TQIDVETSFL 

       250        260        270        280        290        300 
TAPEVRAIME NMIRGLWLNI LGADLGKFPI MTWNEAMTRF GSDKPDLRNP LEIADVADIV 

       310        320        330        340        350        360 
KDVDFKVFAD PANDANGRVS VIRVPNGASI TRKQIDEYTQ FVGIYGAKGL AWLKVNDVNA 

       370        380        390        400        410        420 
GLEGVQSPIA KFLSEEKIKA IFDRTSAQTG DILFFGADKW QIATDAMGAL RLKLGRDLGL 

       430        440        450        460        470        480 
TRLDEWQPLW VIDFPMFECD EEGNLAAMHH PFTSPKDFSP EQLEADPTAA VANAYDMVIN 

       490        500        510        520        530        540 
GYEVGGGSVR IFDPKMQQTV FRILGIDEQQ QREKFGFLLD ALKFGTPPHA GLAFGLDRLT 

       550        560        570        580 
MLLTGTDNIR DVIAFPKTTA AACLMTEAPS FANQQALEEL AITVVTKEE 

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000746 Genomic DNA. Translation: ABR75156.1.
RefSeqYP_001345091.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6VQA9.

Genome annotation databases

GeneID5349358.
GenomeReviewsGene locus Asuc_1805 in contig CP000746_GR.
KEGGasu:Asuc_1805.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAVDRRRDH.

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.
IPR020564. Asp-tRNA-synth_IIb_bac-type.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
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.
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_ACTSZ
AccessionPrimary (citable) accession number: A6VQA9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: November 3, 2009
This is version 18 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