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A8ESW7 (SYD_ARCB4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Abu_0776
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

Protein attributes

Sequence length589 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 – 589589Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000057299

Sequences

Sequence LengthMass (Da)Tools
A8ESW7 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 0A7749D552945D5B

FASTA58967,053
        10         20         30         40         50         60 
MRTHYCTDVT EKLIGQTVTV AGWVNSRRDH GGIIFIDLRD KSGLVQLVAD PQDCKDALAI 

        70         80         90        100        110        120 
AETVRDEFVL IATGKVRARG EGLENPNLIT GKIEIILENL VIENRSRPMP FDINDEKVND 

       130        140        150        160        170        180 
EIKLRNRFLE LRSKKSFDIF QLRSKATIQA RNTLDELGFL DVETPILTKS TPEGARDYLV 

       190        200        210        220        230        240 
PSRVHAGEFY ALPQSPQLFK QLLMVAGFDK YFQIAKCFRD EDLRADRQPE FTQIDVEMSF 

       250        260        270        280        290        300 
CNQEDVIKVA EKLIYDIFTK CGKNVPSTFR RMKYSEAMEK YGSDKPDLRF DMPLVDVIDI 

       310        320        330        340        350        360 
FANSTNEIFA EIAKDKKNNR IKALKCKNGD NIFSKRQMKS FEDYVRKFGA KGLGYFQMKE 

       370        380        390        400        410        420 
DGLKGPLTKF FSEADLEEII KVTELEVGDV VFFGAGAKKV VWDYMGRFRL FLANEMNIVP 

       430        440        450        460        470        480 
KDAYEFLWVI DFPMFEVEDG RTKALHHPFT MPNVEKYDLD NIEDLEEIES IAYDIVLNGT 

       490        500        510        520        530        540 
ELGGGSIRIH KEEIQSKVFK LMGISQEEAK EKFGFLLDAL SYGAPSHGGF ALGLDRMIML 

       550        560        570        580 
LAGTDSIRDV IAFPKTQKAQ CLLTQAPSAV DEEQLKELSI RIRKTVVDS 

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM4018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000361 Genomic DNA. Translation: ABV67041.1.
RefSeqYP_001489710.1. NC_009850.1.

3D structure databases

ProteinModelPortalA8ESW7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8ESW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5624899.
GenomeReviewsGene locus Abu_0776 in contig CP000361_GR.
KEGGabu:Abu_0776.
PATRIC20962920. VBIArcBut20197_0765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHBG396032.
OMAAFPKTQQ.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycABUT367737:ABU_0776-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_ARCB4
AccessionPrimary (citable) accession number: A8ESW7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 34 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