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Q9KDG1 (SYD_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. 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:BH1252
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length595 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 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 – 595595Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_0000110825

Sequences

Sequence LengthMass (Da)Tools
Q9KDG1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3B08EB2EE928883B

FASTA59567,222
        10         20         30         40         50         60 
MIGRTHHCGQ LSEEQVNERV QLKGWVQRRR DLGQVIFVDL RDRSGVVQLV FNSDISQEAL 

        70         80         90        100        110        120 
ETAEKVRNEY VLDVEGVVLK RDPSTVNDKI ATGTIEVHVE RLTILNKAKS LPFQIEANTD 

       130        140        150        160        170        180 
ASEDIRLKYR YLDLRRPDMQ ETMKLRHQTT KLIRDFLDGQ EFFEIETPML TKSTPEGARD 

       190        200        210        220        230        240 
YLVPSRVHHG EFYALPQSPQ IFKQLLMVSG FERYYQIVRC FRDEDLRADR QPEFTQIDIE 

       250        260        270        280        290        300 
TSFMDKEDLL TMTENMMAKI MKEVKGLDVA LPFPRMTYDD AMNRYGSDKP DTRFEMELIE 

       310        320        330        340        350        360 
LSDIVKDSDF KVFSSAIKSG GIVKGLNLKG GAGSLSRKEI DGLAEFVKPY GAKGLAWLKV 

       370        380        390        400        410        420 
EEGELKGPIA KFFAGETGAE LQQAMGAEDG DLLFFAADKK EVVFDSLGAL RLKLGKDFNL 

       430        440        450        460        470        480 
IDESKFNFLW VVDFPLVEYD EEAKRFVALH HPFTSPKQED LTKLETDPAS VRADAYDLVL 

       490        500        510        520        530        540 
NGYELGGGSQ RIYQRPVQEK MFAALGFTEE AAQKEFGFLL EAFEYGTPPH GGIALGLDRL 

       550        560        570        580        590 
VMLLAGRLNL RDTIAFPKTA SASCLLTEAP GEVSLEQLLD LNLSIIGHKP DKVNV 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB04971.1.
PIRD83806.
RefSeqNP_242118.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KDG1.
SMRQ9KDG1. Positions 4-586.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000052564; EBBACP00000051203; EBBACG00000052555.
GeneID892043.
GenomeReviewsGene locus BH1252 in contig BA000004_GR.
KEGGbha:BH1252.
NMPDRfig|272558.1.peg.1252.
PATRIC18939562. VBIBacHal18977_1299.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000858.
HOGENOMHBG396032.
OMAAFPKTQQ.
PhylomeDBQ9KDG1.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycBHAL272558:BH1252-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_BACHD
AccessionPrimary (citable) accession number: Q9KDG1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 79 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