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Reviewed, UniProtKB/Swiss-Prot A1UT52 (SYD_BARBK)

Last modified November 3, 2009. Version 25. 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: BARBAKC583_0868
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length596 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 – 596596Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_1000006638

Sequences

Sequence LengthMass (Da)Tools
A1UT52-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: CCA6AF3F11566C6E

FASTA59667,562
        10         20         30         40         50         60 
MHRYRSHNCA ALRKCDVGTQ VRLSGWVHRV RDHGGILFVD LRDHFGITQI VVNPDSSAFQ 

        70         80         90        100        110        120 
IMEKVRSEWV ICVDGKVCAR SDEVINTTLP TGEIEIFADE IEILSKSDEL PLPVFGEPDY 

       130        140        150        160        170        180 
PEDIRLKYRF LDLRRVTMHK NIMRRTEIIS SIRRHMQDSG FTEFTTPLLT ASSPEGARDF 

       190        200        210        220        230        240 
LVPSRIHQGK FYALPQAPQQ YKQLLMMSGF DRYFQIAPCF RDEDPRADRL PGEFYQLDIE 

       250        260        270        280        290        300 
MSFVEQEDVL ATMEPIIRSV FEEFSDGKLV TQSFPRISYD EAMRKYGSDK PDLRNPIIIE 

       310        320        330        340        350        360 
DVSQHFYDSD FKVFAQILAN NENAQVWAIP AKTGGNRAFC DRMNGWAQGE GQPGLGYIFW 

       370        380        390        400        410        420 
RKEGENFEGA GPIAKNIGEQ RTEAIRTQLG LKEGDACFFV AGDPKKFASF AGASRTRIGE 

       430        440        450        460        470        480 
ELDLIDSKCF SFAWIVDFPF FEWNEDEKKI DFAHNPFSMP QGGMNAVDSQ DPLTIKAFQY 

       490        500        510        520        530        540 
DLVCNGYEIA SGGIRNHSPE MMLKVFNLAG LSREIVEERF GGLYRAFHYG APPHGGMAAG 

       550        560        570        580        590 
VDRIVMLLQG VKNLREISLF PMNQQALDLL MSAPSDVSAT QLNDLGIRIF PKVNNA 

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000524 Genomic DNA. Translation: ABM44906.1.
RefSeqYP_989155.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1UT52.

Genome annotation databases

GeneID4685154.
GenomeReviewsGene locus BARBAKC583_0868 in contig CP000524_GR.
KEGGbbk:BARBAKC583_0868.
NMPDRfig|360095.3.peg.876.
TIGRBARBAKC583_0868.

Phylogenomic databases

OMAYQLDVEM.

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_BARBK
AccessionPrimary (citable) accession number: A1UT52
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 25 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