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B7I8M5 (SYD_ACIB5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate--tRNA ligase

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:aspS
Ordered Locus Names:AB57_3398
OrganismAcinetobacter baumannii (strain AB0057) [Complete proteome] [HAMAP]
Taxonomic identifier480119 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length592 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_B

Subunit structure

Homodimer By similarity. HAMAP MF_00044_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00044_B.

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 processtRNA aminoacylation for protein translation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000198946

Sequences

Sequence LengthMass (Da)Tools
B7I8M5 [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].
Strain: AB0057.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001182 Genomic DNA. Translation: ACJ41968.1.
RefSeqYP_002320704.1. NC_011586.1.

3D structure databases

ProteinModelPortalB7I8M5.
SMRB7I8M5. Positions 2-585.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7I8M5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7046338.
GenomeReviewsGene locus AB57_3398 in contig CP001182_GR.
KEGGabn:AB57_3398.
PATRIC20700461. VBIAciBau111166_3265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAAFPKTQQ.
ProtClustDBPRK00476.

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.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01876.
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.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. AspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_ACIB5
AccessionPrimary (citable) accession number: B7I8M5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families