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Q2YNA7 (SYDND_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 61. 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(Asp/Asn) ligase

EC=6.1.1.23
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Non-discriminating aspartyl-tRNA synthetase
Short name=ND-AspRS
Gene names
Name:aspS
Ordered Locus Names:BAB1_0775
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn) By similarity. HAMAP-Rule MF_00044

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00044

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00044.

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: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aspartate-tRNA(Asn) ligase activity

Inferred from electronic annotation. Source: UniProtKB-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(Asp/Asn) ligase HAMAP-Rule MF_00044
PRO_0000235512

Regions

Nucleotide binding221 – 2233ATP By similarity
Nucleotide binding540 – 5434ATP By similarity
Region199 – 2024Aspartate By similarity

Sites

Binding site1751Aspartate By similarity
Binding site2211Aspartate By similarity
Binding site4541Aspartate By similarity
Binding site4881ATP By similarity
Binding site4911Aspartate By similarity
Binding site4951Aspartate By similarity
Site331Important for tRNA non-discrimination By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YNA7 [UniParc].

Last modified February 7, 2006. 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]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ10731.1.
RefSeqYP_414208.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YNA7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_0775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ10731; CAJ10731; BAB1_0775.
GeneID3788627.
KEGGbmf:BAB1_0775.
PATRIC17844455. VBIBruMel86222_0809.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHOG000275160.
KOK01876.
OMASLSRKQI.
OrthoDBEOG68Q0NX.

Enzyme and pathway databases

BioCycBABO359391:GKDV-786-MONOMER.
BMEL359391:GJOQ-786-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPMF_00044. Asp_tRNA_synth.
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF5. PTHR22594:SF5. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYDND_BRUA2
AccessionPrimary (citable) accession number: Q2YNA7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names