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Reviewed, UniProtKB/Swiss-Prot Q81LI7 (SYD_BACAN)

Last modified February 9, 2010. Version 54. 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
Synonyms: aspS-2
Ordered Locus Names: BA_4632, GBAA_4632, BAS4297
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [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

Subunit structure

Homodimer By similarity. HAMAP MF_00044

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 – 591591Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_0000110820

Sequences

Sequence LengthMass (Da)Tools
Q81LI7-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 905F62B70A5BA470

FASTA59166,294
        10         20         30         40         50         60 
MAERTHACGK VTVEAVGQTV QLKGWVQKRR DLGGLIFIDL RDRTGIVQVV FNPETSKEAL 

        70         80         90        100        110        120 
EVAETIRSEY VLHVEGTVVE RGEGAINDNM ATGRIEVQAT KVSVLNAAKT 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 KFFGEEDASV LMNTLEATAG 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 LNLKLNVKEE K 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP28335.1.
AE017334 Genomic DNA. Translation: AAT33754.1.
AE017225 Genomic DNA. Translation: AAT56596.1.
RefSeqNP_846849.1.
YP_021279.1.
YP_030545.1.

3D structure databases

SMRQ81LI7. Positions 4-585.
ModBaseSearch...

Genome annotation databases

GeneID1085460.
2814871.
2850462.
GenomeReviewsGene locus BA_4632 in contig AE016879_GR.
Gene locus BAS4297 in contig AE017225_GR.
Gene locus GBAA_4632 in contig AE017334_GR.
KEGGban:BA4632.
bar:GBAA4632.
bat:BAS4297.
TIGRBA_4632.
GBAA_4632.

Phylogenomic databases

HOGENOMHBG396032.
OMAPLFEYDE.

Enzyme and pathway databases

BioCycBANT260799:BAS4297-MONOMER.
BANT261594:GBAA4632-MONOMER.
BRENDA6.1.1.12. 267517.

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_cons-dom.
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.
IPR016027. NA-bd_OB-fold-like.
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_BACAN
AccessionPrimary (citable) accession number: Q81LI7
Secondary accession number(s): Q6HSZ3, Q6KM82
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: February 9, 2010
This is version 54 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