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A4SPN5 (SYD_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:ASA_2844
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length588 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 – 588588Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000006629

Sequences

Sequence LengthMass (Da)Tools
A4SPN5 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: B50A008E8D9EE40B

FASTA58865,386
        10         20         30         40         50         60 
MRSIYCGQVN EAHAGQTITL CGWVHRRRDL GGLIFIDMRD REGIVQVFFD PDKPDAFALA 

        70         80         90        100        110        120 
SELRGEFCIQ VSGVVRTRPD SQRNSDMATG AIEVFAHELT IINRAEPLPL DFNQVNSEEQ 

       130        140        150        160        170        180 
RLKFRYLDLR RPEMAKYLKT RAKASAFVRR FMDEHGFLDI ETPMLTKATP EGARDYLVPS 

       190        200        210        220        230        240 
RVHKGKFYAL PQSPQLFKQL LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT 

       250        260        270        280        290        300 
APQVRELMEE MIRNLWQHVL AVDLGDFPVM TFDEAMRRFG SDKPDLRLPM ELVDVADLLT 

       310        320        330        340        350        360 
AVEFAVFAGP ANDPKGRVAA LKVPGGAELS RKQIDEYTKF VGIYGAKGLA WMKVNEAANG 

       370        380        390        400        410        420 
IEGVQSPVAK FLSDEIVREI LARTGAADGD IIFFGADSKK VVADAIGALR LKVGRDLGLM 

       430        440        450        460        470        480 
ENSWKPLWVI DFPMFEEDSE GGLAAMHHPF TAPSNLGPSE LKANPLSAYA NAYDMVINGY 

       490        500        510        520        530        540 
EVGGGSVRIH NSEMQATVFD ILGITPAEQR LKFGFLLDAL KYGTPPHAGL AFGLDRLSML 

       550        560        570        580 
LTGTDNIRDV IAFPKTTAAA CLMTDAPSFA NQAQMSELAI ATTVKGDE 

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed: 18801193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000644 Genomic DNA. Translation: ABO90857.1.
RefSeqYP_001142605.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SPN5.
SMRA4SPN5. Positions 1-580.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SPN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4996162.
GenomeReviewsGene locus ASA_2844 in contig CP000644_GR.
KEGGasa:ASA_2844.
PATRIC20792095. VBIAerSal2987_2822.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHBG396032.
OMAAFPKTQQ.
PhylomeDBA4SPN5.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycASAL382245:ASA_2844-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_AERS4
AccessionPrimary (citable) accession number: A4SPN5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 40 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