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Reviewed, UniProtKB/Swiss-Prot Q5WHP3 (SYD_BACSK)

Last modified November 3, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aspartyl-tRNA synthetase
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
Gene names
Name: aspS
Ordered Locus Names: ABC1577
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm. HAMAP MF_00044

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 processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 589589Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_0000110828

Sequences

Sequence LengthMass (Da)Tools
Q5WHP3-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: BF9C8E7E4AB71F4C

FASTA58966,682
        10         20         30         40         50         60 
MKRTHHCGQL DKTLAGQQVQ LKGWVQRRRD LGQVIFLDLR DRSGIVQVVC SPEVSEEALK 

        70         80         90        100        110        120 
AADRVRNEYL VAVSGIVVER NEQAVNDKLA TGAIEVHVRE LEILNVSKSL PFQIEADTDA 

       130        140        150        160        170        180 
AEDVRLKYRY LDLRRPDMQE AFAMRHKIMK SVRDFLDADG YLEIETPMLT KSTPEGARDY 

       190        200        210        220        230        240 
LVPSRVHHGQ FYALPQSPQI FKQLLMVSGF EKYFQIVRCF RDEDLRADRQ PEFTQIDIET 

       250        260        270        280        290        300 
SFLDTEDILA MTEAMMEKLL KETHGLELKR PFSRMTYEEA MNRYGSDKPD TRFGMELIEL 

       310        320        330        340        350        360 
SDVLKDTEFK VFKGALEAGG IIKGLTLKGG ADKLSRKDID ALADFVKPYG AKGLAWLKVD 

       370        380        390        400        410        420 
DEGIKGPIAK FFNEAQTAAL LAAMDAEAGD LLFFGADKKQ VVFHALGALR LKFGKEFQLI 

       430        440        450        460        470        480 
DENAFHFLWV TDFPLVEYDE QAKRFVALHH PFTRPKAEDL DLMETHPEQV RAEAYDLVLN 

       490        500        510        520        530        540 
GFELGGGSQR IYERELQEKM FKLLGFSSEA AKEEFGFLLE AFDYGTPPHG GIALGLDRIV 

       550        560        570        580 
MLLARKSNLR EVIAFPKTAS ASDLLTEAPN KVSVEQLIDL NLSIISKRS 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006627 Genomic DNA. Translation: BAD64112.1.
RefSeqYP_175073.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WHP3.

Genome annotation databases

GeneID3201736.
GenomeReviewsGene locus ABC1577 in contig AP006627_GR.
KEGGbcl:ABC1577.
NMPDRfig|66692.3.peg.1539.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5WHP3.
OMAVDRRRDH.

Enzyme and pathway databases

BioCycBCLA66692:ABC1577-MON.

Family and domain databases

HAMAPMF_00044.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002312. Asp-tRNA-synth_IIb.
IPR020564. Asp-tRNA-synth_IIb_bac-type.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA_bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
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.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_BACSK
AccessionPrimary (citable) accession number: Q5WHP3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: November 23, 2004
Last modified: November 3, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents