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Reviewed, UniProtKB/Swiss-Prot Q5R9I5 (SYDC_PONAB)

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, cytoplasmic
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
Gene names
Name: DARS
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).

Subunit structure

Homodimer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro 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
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processaspartyl-tRNA aminoacylation

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 – 501501Aspartyl-tRNA synthetase, cytoplasmic
PRO_0000250735

Regions

Region411 – 4155Binding site for the 3'-end of tRNA Potential

Amino acid modifications

Modified residue2381Phosphoserine By similarity
Modified residue5001Phosphothreonine; by PKA Potential

Sequences

Sequence LengthMass (Da)Tools
Q5R9I5-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: A72C205B15817901

FASTA50157,228
        10         20         30         40         50         60 
MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK SDRVLVRVRD LTIQKADEVV 

        70         80         90        100        110        120 
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV 

       130        140        150        160        170        180 
RKVNQKIESC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL 

       190        200        210        220        230        240 
DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF 

       250        260        270        280        290        300 
KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 

       310        320        330        340        350        360 
EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV 

       370        380        390        400        410        420 
EMGDEDDLST PNEKLLGHLI KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 

       430        440        450        460        470        480 
RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF 

       490        500 
LGLHNVRQTS MFPRDPKRLT P 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

CR859403 mRNA. Translation: CAH91575.1.
RefSeqNP_001125925.1.
UniGenePab.19002

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID100172859.

Phylogenomic databases

HOVERGENQ5R9I5.

Enzyme and pathway databases

BRENDA6.1.1.12. 269192.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002312. Asp-tRNA-synth_IIb.
IPR004523. Asp-tRNA-synth_IIb_arc/euk.
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.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00458. aspS_arch. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYDC_PONAB
AccessionPrimary (citable) accession number: Q5R9I5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 21, 2004
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 projectHPI (Human Proteome Initiative)

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