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B7IIR4 (SYD_BACC2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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:BCG9842_B0714
OrganismBacillus cereus (strain G9842) [Complete proteome] [HAMAP]
Taxonomic identifier405531 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length591 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 – 591591Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000198960

Sequences

Sequence LengthMass (Da)Tools
B7IIR4 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 56ADE9E090CA0C00

FASTA59166,322
        10         20         30         40         50         60 
MAERTHACGK VTVEAVGQTV QLKGWVQKRR DLGGLIFIDL RDRTGIVQVV FNPETSKEAL 

        70         80         90        100        110        120 
EVAETIRSEY VLHVEGTVVE RGEGAINDNM ATGRIEVQAT KVNVLNAAKT TPIIIADDTD 

       130        140        150        160        170        180 
ASEDVRLKYR YLDLRRPVMF NTFKMRHDVT KTIRNFLDTE EFLEVETPIL TKSTPEGARD 

       190        200        210        220        230        240 
YLVPSRVHDG EFYALPQSPQ LFKQLLMVGG FERYYQVARC FRDEDLRADR QPEFTQIDIE 

       250        260        270        280        290        300 
ASFLTQDEIL DMMERMMTKV MKDAKGVEVS APFPRMKYAD AMARYGSDKP DTRFEMELTD 

       310        320        330        340        350        360 
LSEFAAGCGF KVFTSAVESG GQVKAINAKG AASKYSRKDI DALTEFVKVY GAKGLAWLKV 

       370        380        390        400        410        420 
EEDGLKGPIA KFFGEEDANV LMTTLEATAG DLLLFVADKK SVVADSLGAL RLRLGKELEL 

       430        440        450        460        470        480 
IDESKFNFLW VTDWPLLEYD EDADRYFAAH HPFTMPFRED VELLETAPEK ARAQAYDLVL 

       490        500        510        520        530        540 
NGYELGGGSL RIYERDVQEK MFKALGFSQE EAQEQFGFLL EAFEYGTPPH GGIALGLDRL 

       550        560        570        580        590 
VMLLAGRTNL RDTIAFPKTA SASCLLTEAP SPVAEAQLEE LNLKLSLKEE K 

« Hide

References

[1]"Genome sequence of Bacillus cereus G9842."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G9842.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001186 Genomic DNA. Translation: ACK97064.1.
RefSeqYP_002447982.1. NC_011772.1.

3D structure databases

ProteinModelPortalB7IIR4.
SMRB7IIR4. Positions 4-585.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7IIR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000106333; EBBACP00000098181; EBBACG00000106326.
GeneID7186043.
GenomeReviewsGene locus BCG9842_B0714 in contig CP001186_GR.
KEGGbcg:BCG9842_B0714.
PATRIC18904576. VBIBacCer50903_4438.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000858.
HOGENOMHBG396032.
OMAAFPKTQQ.
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_BACC2
AccessionPrimary (citable) accession number: B7IIR4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 26 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