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B0SWQ6 (SYD_CAUSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:Caul_2557
OrganismCaulobacter sp. (strain K31) [Complete proteome] [HAMAP]
Taxonomic identifier366602 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length609 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 – 609609Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000074694

Sequences

Sequence LengthMass (Da)Tools
B0SWQ6 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 82ECE8C71554B9F0

FASTA60968,147
        10         20         30         40         50         60 
MHAYRTHTCG ALRASDTGAS VRVSGWIHRK RDHGGLVFID LRDHYGLTQL VLHPETPGFD 

        70         80         90        100        110        120 
VVERLRAESV IKIDGEVVAR DAAAVNPNLP TGEIEIRVSA VEVLSEAAEL PLPVFGEPDY 

       130        140        150        160        170        180 
PEEIRLKHRY LDLRRETLHK NIVLRSRVIQ SIRSRMFAQG FNEFQTPILT ASSPEGARDF 

       190        200        210        220        230        240 
LVPSRLHPGK FYALPQAPQQ FKQLLMVSGF DRYFQIAPCF RDEDLRADRS LEFYQLDVEM 

       250        260        270        280        290        300 
SFVTQEDVFA AIEPVMHGVF EEFSAGKPVS PIDGVHTFTN DFGATLEHRG FERLTYAQSM 

       310        320        330        340        350        360 
AWYGSDKPDL RNPIKMQDVS EHFRDGGFGL FAKILGADPK NRVWAIPAPT GGSRAFCDRM 

       370        380        390        400        410        420 
NSWAQGEGQP GLGYAFFSKD QNGWGGPIAK NLGEGFQPIA DQLGLTHDDA VFFVAGDPAV 

       430        440        450        460        470        480 
FAKFAGLART RVGTELKLVD EEQFKFCWIV DFPMFEWNED EKKVDFSHNP FSMPQGGLEA 

       490        500        510        520        530        540 
LETQDPLTIR AYQYDIVCNG YELCSGAIRN HKPEIMLKAF EVAGYGAEVV EEQFGGMLNA 

       550        560        570        580        590        600 
FRYGAPPHGG LAPGIDRIVM LLAEQVAIRE VIAFPLNQQG QDLLMNAPAE AQDRQYKELY 


IRSAPPIKV 

« Hide

References

[1]"Complete sequence of chromosome of Caulobacter sp. K31."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Stephens C., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000927 Genomic DNA. Translation: ABZ71684.1.
RefSeqYP_001684182.1. NC_010338.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB0SWQ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5900012.
GenomeReviewsGene locus Caul_2557 in contig CP000927_GR.
KEGGcak:Caul_2557.
PATRIC21318180. VBICauSp18104_2948.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAYQLDVEM.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycCSP78:CAUL_2557-MONOMER.

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_CAUSK
AccessionPrimary (citable) accession number: B0SWQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 30 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