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Reviewed, UniProtKB/Swiss-Prot Q1LTF0 (SYD_BAUCH)

Last modified June 16, 2009. Version 28. 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: BCI_0315
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

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 By similarity.

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_1000006639

Sequences

Sequence LengthMass (Da)Tools
Q1LTF0-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 52E7422E511E9BF2

FASTA58967,501
        10         20         30         40         50         60 
MRTIYCGQLN KSHLGQEVIL CGWVYRYRNL GRLIFIELSD REGRVQVVFD LTHPSIFSNA 

        70         80         90        100        110        120 
AKLRNDFCIQ LHGIVRTRLD KQINYNITTG EIEVLATNLT ILNSSQPLPL DINFHNNEEQ 

       130        140        150        160        170        180 
RLKFRYLDLR NPEMAQRLKL RAKITSLVRH FMEKKGFLDI ETPMLTKTTP EGARDYLVPS 

       190        200        210        220        230        240 
RVHKGQFYAL PQSPQLFKQL LMISGFDRYY QIVKCFRDED LRADRQPEFT QIDVEASFIN 

       250        260        270        280        290        300 
AEQICKIMED LVRHLWREIQ EVELENFQYM SYTAAMYRFG SDKPDLRNPI EIVDVVDLVK 

       310        320        330        340        350        360 
NTTCTILADI AKDIKNRVVA LRVPNGAKLS LNDIKKYEKY IQTYGIKFII WMKVYQGKDG 

       370        380        390        400        410        420 
VKTTQSSITK YLLPEDIMSI IERTGACDGD ILFFAAGNNN IINNVMGALR IKLGCDLKLN 

       430        440        450        460        470        480 
RENSWAPLWI VDFPMFEKDD EGNLHAVHHP FTAPKNIDIP TLLQYPLKAK ANAYDMVING 

       490        500        510        520        530        540 
YEVGSGSVRI HCAELQQTIF SILGMTRNEQ SSKFGFFIDA LKYGAPPHAG FAFGLDRLVM 

       550        560        570        580 
LLTSTENIRD VIAFPKTTTA IDLMTEAPSI GNTIALKELS IEILDKNKI 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000238 Genomic DNA. Translation: ABF14266.1.
RefSeqYP_588764.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4056450.
GenomeReviewsGene locus BCI_0315 in contig CP000238_GR.
KEGGbci:BCI_0315.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LTF0.
OMAQ1LTF0. VDRRRDH.

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.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR004115. GAD.
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_BAUCH
AccessionPrimary (citable) accession number: Q1LTF0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 28 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