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Reviewed, UniProtKB/Swiss-Prot B7GWN1 (SYD_ACIB3)

Last modified September 22, 2009. Version 8. 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: ABBFA_000568
OrganismAcinetobacter baumannii (strain AB307-0294) [Complete proteome] [HAMAP]
Taxonomic identifier557600 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

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 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 – 592592Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_1000198947

Sequences

Sequence LengthMass (Da)Tools
B7GWN1-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 627D7614040EA87E

FASTA59266,667
        10         20         30         40         50         60 
MMRTHYCGSL TEAQIDQTVT LCGWVHRRRD HGGVIFLDMR DRDGLVQVVI DPDTPEAFAT 

        70         80         90        100        110        120 
ADKARSEYVL KITGRVRRRY EGTENPNMVS GQIEVLGKEI EVLAASETPP FPLNDDTINV 

       130        140        150        160        170        180 
SEEHRLKYRF LDIRRPEMLE RLRFRSKVTN LIRNYLDDHG FLDVETPILT RATPEGARDY 

       190        200        210        220        230        240 
LVPSRVQNGS FYALPQSPQL FKQLLMVGGI DRYYQIAKCF RDEDLRADRQ PEFTQIDIET 

       250        260        270        280        290        300 
SFLNDDDIMD LMEGMTVKLF NDLLGVKFEK FRRMPYSEAM RDYASDKPDL RIPLKLVDVA 

       310        320        330        340        350        360 
DLMQEVEFKV FAGPAKDPKG RIAALRVPGA GSLTRSQIDE YTKFVGIYGA KGLAYIKVNE 

       370        380        390        400        410        420 
IEKGIEGLQS PIVKFIEPIV MQLLERVGAE NGDIVFFGAD KAKIVNDAMG ALRVKIGHDL 

       430        440        450        460        470        480 
NLATCEWAPL WVVDFPMFEE TDDGKWTSVH HPFTLPKSSV EDVKSNPGEA LSVAYDMVLN 

       490        500        510        520        530        540 
GTEVGGGSLR IYTLEMQKAI FEALGISDEE AEEKFSFLLN ALRYGAPPHG GLAFGLDRLV 

       550        560        570        580        590 
MLMTGATSIR DVIAFPKTKT AECPLTQAPA PVEANQLRDL GIRLREQQKK EA 

« Hide

References

[1]"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii."
Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R.
J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001172 Genomic DNA. Translation: ACJ56458.1.
RefSeqYP_002324492.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7057995.
GenomeReviewsGene locus ABBFA_000568 in contig CP001172_GR.
KEGGabb:ABBFA_000568.

Organism-specific databases

CMRSearch...

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_ACIB3
AccessionPrimary (citable) accession number: B7GWN1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: September 22, 2009
This is version 8 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