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Q3SYZ4 (SYDC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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, cytoplasmic

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:DARS
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

Catalytic activity

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

Subunit structure

Homodimer; also part of a multisubunit complex that groups AIMP1, AIMP2, EEF1A1 and 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
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
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 – 501501Aspartate--tRNA ligase, cytoplasmic
PRO_0000245022

Regions

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

Amino acid modifications

Modified residue741N6-acetyllysine By similarity
Modified residue2381Phosphoserine By similarity
Modified residue2491Phosphoserine By similarity
Modified residue3741N6-acetyllysine By similarity
Modified residue5001Phosphothreonine; by PKA Potential

Sequences

Sequence LengthMass (Da)Tools
Q3SYZ4 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: A8E00861B2C3E607

FASTA50157,036
        10         20         30         40         50         60 
MPSANASRRS QEKPREIMDA AEDYAKERYG VSSMIQSQEK PDRVLVRISD LTVQKAGEVV 

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

       130        140        150        160        170        180 
RKVNQKIGSC TQQDVELHVQ KIYVISSAEP RLPLQLDDAV RPEVEGEEEG RATVNQDTRL 

       190        200        210        220        230        240 
DNRVIDLRTS TSQAIFRLQS GICHPFRETL TNKGFVEIQT PKIISAASEG GANVFTVSYF 

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

       310        320        330        340        350        360 
EVVEEIADTL VQIFKGLQKR FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGI 

       370        380        390        400        410        420 
EMGDEEDLST PNEKLLGRLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 

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

       490        500 
LGLHNVRQTS MFPRDPKRLT P 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC103319 mRNA. Translation: AAI03320.1.
IPIIPI00715362.
RefSeqNP_001030257.1. NM_001035085.1.
UniGeneBt.48837.

3D structure databases

ProteinModelPortalQ3SYZ4.
SMRQ3SYZ4. Positions 22-501.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SYZ4.

Proteomic databases

PRIDEQ3SYZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID510162.
KEGGbta:510162.

Organism-specific databases

CTD1615.

Phylogenomic databases

eggNOGmaNOG08209.
GeneTreeENSGT00550000074880.
HOVERGENHBG001028.
InParanoidQ3SYZ4.
OrthoDBEOG470TH2.
PhylomeDBQ3SYZ4.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA-synth_IIb_arc/euk.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01876.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00458. AspS_arch. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYDC_BOVIN
AccessionPrimary (citable) accession number: Q3SYZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 11, 2005
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families