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Reviewed, UniProtKB/Swiss-Prot Q65GR4 (SYD_BACLD)

Last modified November 3, 2009. Version 40. 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: BLi02881, BL05288
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length592 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 – 592592Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_0000110827

Sequences

Sequence LengthMass (Da)Tools
Q65GR4-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: EBD733AB72A2EAEC

FASTA59266,378
        10         20         30         40         50         60 
MFGRTYYCGE ITEKAIGETV VLKGWVQKRR DLGGLIFIDL RDRTGIVQVV FNPDVSKDAL 

        70         80         90        100        110        120 
ETAESIRSEY VLDITGKVVA REEATVNPNL KTGRIEIQAE SVDVLSAAKT PPFAISDQAA 

       130        140        150        160        170        180 
EVSEDIRLKH RYLDLRRPEM FNSLKMRHNV TKAVRRFLDD NGFLDIETPV LTKSTPEGAR 

       190        200        210        220        230        240 
DYLVPSRVHE GEFYALPQSP QIFKQLLMVS GFDRYYQIAR CFRDEDLRAD RQPEFTQIDI 

       250        260        270        280        290        300 
EMSFMSQEDI MKLSEEMMAH VMRETHGIEI SLPLPRMSYE DAMNRYGSDK PDTRFGMLLT 

       310        320        330        340        350        360 
DVSEAVKDSD FKVFASAVAN GGAVKAINVK GAAANYSRKD IDALGEFAAN YGAKGLAWLK 

       370        380        390        400        410        420 
TEADGLKGPI AKFFAGEKQE ALVQALDAAD GDLLLFVADK LEVANDALGA LRLKLGKELN 

       430        440        450        460        470        480 
LIDESLFNFL WVVDWPLLEY DAEEGRYYAA HHPFTMPVRE DLKLIETNPQ DMKAQAYDLV 

       490        500        510        520        530        540 
LNGYELGGGS IRIFEKDVQE KMFGLLGFSE EEAKEQFGFL LEAFDYGAPP HGGIALGLDR 

       550        560        570        580        590 
LVMLLSGRTN LRDTIAFPKT ASASCLMTEA PSEVDNAQLD ELHLEIKRKI RQ 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017333 Genomic DNA. Translation: AAU41750.1.
CP000002 Genomic DNA. Translation: AAU24387.1.
RefSeqYP_080025.1.
YP_092443.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ65GR4.

Genome annotation databases

GeneID3029050.
3098196.
GenomeReviewsGene locus BLi02881 in contig AE017333_GR.
Gene locus BL05288 in contig CP000002_GR.
KEGGbld:BLi02881.
bli:BL05288.
NMPDRfig|279010.5.peg.3209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ65GR4.
OMAVDRRRDH.

Enzyme and pathway databases

BioCycBLIC279010:BL05288-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_BACLD
AccessionPrimary (citable) accession number: Q65GR4
Secondary accession number(s): Q62S73
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 40 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