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B2S501 (SYD_BRUA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:BAbS19_I07240
OrganismBrucella abortus (strain S19) [Complete proteome] [HAMAP]
Taxonomic identifier430066 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length595 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 By similarity 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
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 – 595595Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000090966

Sequences

Sequence LengthMass (Da)Tools
B2S501 [UniParc].

Last modified July 1, 2008. 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]"Genome sequence of Brucella abortus vaccine strain S19 compared to virulent strains yields candidate virulence genes."
Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.
PLoS ONE 3:E2193-E2193(2008) [PubMed: 18478107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000887 Genomic DNA. Translation: ACD72248.1.
RefSeqYP_001934722.1. NC_010742.1.

3D structure databases

ProteinModelPortalB2S501.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2S501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6327883.
GenomeReviewsGene locus BAbS19_I07240 in contig CP000887_GR.
KEGGbmc:BAbS19_I07240.
PATRIC17818482. VBIBruAbo38055_2014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAYQLDVEM.
ProtClustDBPRK00476.

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_BRUA1
AccessionPrimary (citable) accession number: B2S501
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 30 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