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A7GT84 (SYD_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:Bcer98_3118
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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_1000074690

Sequences

Sequence LengthMass (Da)Tools
A7GT84 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: C784E1F4C2E2CA7A

FASTA58966,065
        10         20         30         40         50         60 
MAERTHACGR VTVEAIGQTV QLKGWVQKRR DLGGLIFIDL RDRTGIVQVV FSPETSKEAL 

        70         80         90        100        110        120 
EVAETIRGEY VLHVEGTVVA RGAGAINENM ATGQIEVQAT KVTVLNAAKT TPIIIADDTD 

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

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

       250        260        270        280        290        300 
ASFLTQEEIL DMMERMMTKV MKDVKGVEIS VPFPRMTYAD AMARYGSDKP DTRFEMELTD 

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

       370        380        390        400        410        420 
EEDGLKGPIA KFFNEEEANV IMTTLEASAG DLLLFVADKK SVVADSLGAL RLRLGKELEL 

       430        440        450        460        470        480 
IDENKFNFLW VTDWPLLEYD EEANRYFAAH HPFTMPFRED VELLETAPEK ARAQAYDLVL 

       490        500        510        520        530        540 
NGYELGGGSL RIYERDVQEK MFKALGFTQE EAREQFGFLL EAFEYGTPPH GGIALGLDRL 

       550        560        570        580 
VMLLAGRTNL RDTIAFPKTA SASCLLTDAP SPVAGAQLEE LHLKLNVKE 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS23342.1.
RefSeqYP_001376337.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GT84.
SMRA7GT84. Positions 4-585.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GT84.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000038158; EBBACP00000037209; EBBACG00000038149.
GeneID5346047.
GenomeReviewsGene locus Bcer98_3118 in contig CP000764_GR.
KEGGbcy:Bcer98_3118.
PATRIC18934866. VBIBacCyt128034_3276.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
GeneTreeEBGT00050000000858.
HOGENOMHBG396032.
OMAAFPKTQQ.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycBCER315749:BCER98_3118-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_BACCN
AccessionPrimary (citable) accession number: A7GT84
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 39 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