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Reviewed, UniProtKB/Swiss-Prot Q57DZ8 (SYD_BRUAB)

Last modified November 25, 2008. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: BruAb1_0768
OrganismBrucella abortus [Complete proteome] [HAMAP]
Taxonomic identifier235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length595 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).

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

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: HAMAP

   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 – 595595Aspartyl-tRNA synthetase
PRO_0000235511

Sequences

Sequence LengthMass (Da)Tools
Q57DZ8-1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 6CAE4EDFF3F69E50

FASTA59567,255
        10         20         30         40         50         60 
MHRYRSHTCA ALRKTDVGSN VRLSGWVHRV RDHGGILFID LRDHYGITQI VADPDSPAFK 

        70         80         90        100        110        120 
VAETVRGEWV IRVDGEVKAR ADDAVNTNLP TGEVEIFATE IEVLSPAKEL PLPVFGEPDY 

       130        140        150        160        170        180 
PEDIRLKYRF LDLRRETLHK NIMSRTKIIA AMRRRMTEIG FNEFSTPILT ASSPEGARDF 

       190        200        210        220        230        240 
LVPSRIHPGK FYALPQAPQQ YKQLLMVAGF DRYFQIAPCF RDEDPRADRL PGEFYQLDLE 

       250        260        270        280        290        300 
MSFVTQEEVW ETMEPVMRGI FEEFAEGKPV TKVFRRIAYD DAIRTYGSDK PDLRNPIEMQ 

       310        320        330        340        350        360 
AVTDHFAGSG FKVFANMIAN DAKVEVWAIP AKTGGSRAFC DRMNSWAQSE GQPGLGYIFW 

       370        380        390        400        410        420 
RKEGDKLEGA GPIAKNIGEE RTEAIRKQMG LEDGDACFFV AGLPSKFYKF AGDARTRAGE 

       430        440        450        460        470        480 
ELNLVDRDRF ELAWIIDFPF YEWDEDNKKI DFAHNPFSLP QGGMDALENM DPLEIKAYQY 

       490        500        510        520        530        540 
DLVCNGFEIA SGSIRNQLPE VMVKAFEKVG LSQQDVEERF GGLYRAFQYG APPHGGMAAG 

       550        560        570        580        590 
IDRVIMLLVG AKNLREISLF PMNQQALDLL MGAPSEVSPA QLRDLHVRLA PVQKS 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941 / Biovar 1.

Cross-references

Sequence databases

AE017223 Genomic DNA. Translation: AAX74136.1.
RefSeqYP_221497.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3339422.
GenomeReviewsGene locus BruAb1_0768 in contig AE017223_GR.
KEGGbmb:BruAb1_0768.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ57DZ8.

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_0768-MON.

Family and domain databases

HAMAPMF_00044.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR006195. aa-tRNA-synth_II.
IPR002312. Asp-tRNA-synth_IIb.
IPR004524. Asp-tRNA-synth_IIb_bac/mito.
IPR004115. GAD.
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_BRUAB
AccessionPrimary (citable) accession number: Q57DZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 10, 2005
Last modified: November 25, 2008
This is version 28 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

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

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