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P15178 (SYDC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:Drs1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Aspartate--tRNA ligase, cytoplasmic
PRO_0000111012

Amino acid modifications

Modified residue741N6-acetyllysine By similarity
Modified residue2381Phosphoserine By similarity
Modified residue2491Phosphoserine By similarity
Modified residue3741N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P15178 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: D3D389B39D7327E2

FASTA50157,126
        10         20         30         40         50         60 
MPSANASRKG QEKPREIVDA AEDYAKERYG VSSMIQSQEK PDRVLVRVKD LTVQKADEVV 

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

       130        140        150        160        170        180 
RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAI RPEVEGEEDG RATVNQDTRL 

       190        200        210        220        230        240 
DNRIIDLRTS TSQAIFHLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF 

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

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

       370        380        390        400        410        420 
EMDDEEDLST PNEKLLGRLV KEKYDTDFYV LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 

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

       490        500 
LGLHNVRQTS MFPRDPKRLT P

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and primary structure of cDNA encoding the catalytic domain of rat liver aspartyl-tRNA synthetase."
Mirande M., Waller J.-P.
J. Biol. Chem. 264:842-847(1989) [PubMed: 2642907] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Genomic organization of the rat aspartyl-tRNA synthetase gene family: a single active gene and several retropseudogenes."
Lazard M., Agou F., Cavarelli J., Latreille M.T., Moras D., Mirande M.
Gene 180:197-205(1996) [PubMed: 8973367] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04487 mRNA. Translation: AAA40789.1.
U30812 expand/collapse EMBL AC list , U30485, U30800, U30801, U30802, U30803, U30804, U30805, U30806, U30807, U30808, U30809, U30810, U30811 Genomic DNA. Translation: AAC52981.1.
BC072534 mRNA. Translation: AAH72534.1.
IPIIPI00206224.
PIRSYRTDT. A32197.
RefSeqNP_446251.1. NM_053799.2.
UniGeneRn.2388.

3D structure databases

ProteinModelPortalP15178.
SMRP15178. Positions 22-501.
ModBaseSearch...

Protein-protein interaction databases

IntActP15178. 1 interaction.
STRINGP15178.

Proteomic databases

PRIDEP15178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000005127; ENSRNOP00000005127; ENSRNOG00000003743.
GeneID116483.
KEGGrno:116483.
NMPDRfig|10116.3.peg.9015.
UCSCBC072534. rat.

Organism-specific databases

CTD1615.
RGD621167. Dars.

Phylogenomic databases

eggNOGroNOG09672.
GeneTreeENSGT00550000074880.
HOVERGENHBG001028.
InParanoidP15178.
OMARNPKQSN.
OrthoDBEOG470TH2.
PhylomeDBP15178.

Gene expression databases

ArrayExpressP15178.
GenevestigatorP15178.
GermOnlineENSRNOG00000003743. Rattus norvegicus.

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...

Other

NextBio619059.

Entry information

Entry nameSYDC_RAT
AccessionPrimary (citable) accession number: P15178
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: January 25, 2012
This is version 98 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

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