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Reviewed, UniProtKB/Swiss-Prot Q3KRD0 (SYDM_RAT)

Last modified February 9, 2010. Version 44. 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, mitochondrial
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
Gene names
Name: Dars2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Gene Ontology (GO)
   Biological processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

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

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 652606Aspartyl-tRNA synthetase, mitochondrial
PRO_0000250738

Amino acid modifications

Modified residue6261N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3KRD0-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 6CB570CC05F30086

FASTA65273,953
        10         20         30         40         50         60 
MYLGSWLNRL GRGLSRPIGK TKQPIWGSLS RSLTLSSQRV PEFSSFVART NTCGELRSSH 

        70         80         90        100        110        120 
LGQEVTLCGW IQYRRQNTFL VLRDCHGLVQ ILIPQDESAA SVRRTLCEAP VESVVRVSGT 

       130        140        150        160        170        180 
VIARPLGQEN PKMPTGEIEI KAKTAELLNA CKKLPFEIKD FVKKTEALRL QYRYLDLRSS 

       190        200        210        220        230        240 
QMQHNLRLRS QMVMKMREYL CTLHGFVDIE TPTLFKRTPG GAKEFLVPSR EPGRFYSLPQ 

       250        260        270        280        290        300 
SPQQFKQLLM VGGLDRYFQV ARCYRDEGSR PDRQPEFTQI DIEMSFVDQT GIQHLVEGLL 

       310        320        330        340        350        360 
HYSWPEDKDP LVAPFPSMTF AEALATYGTD KPDTRFGMKI VDISDVFRNT EIRFLQDALA 

       370        380        390        400        410        420 
KPQGTVKAIC VHEGAKYLRK EDIEFIRKFA AHHFSQEVLP IFLNARKNWS SPFAKFITEE 

       430        440        450        460        470        480 
ERLELTRLME IQEDDMVLLT AGQHEKACSL LGKLRLECAD LLETRGLALR DPALFSFLWV 

       490        500        510        520        530        540 
LDFPLFLAKE ESPTELESAH HPFTAPHPGD IHLLYTEPEK VRGQHYDLVL NGNEIGGGSI 

       550        560        570        580        590        600 
RIHDAQLQRY ILETLLKEDV KLLSHLLQAL DYGAPPHGGI ALGLDRLVCL VTGAPSIRDV 

       610        620        630        640        650 
IAFPKSYRGH DLMSNAPDTV SPEDLKPYHI HVSWPTDSEE RASATPSKYL SS 

« Hide

References

[1]"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: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC105774 mRNA. Translation: AAI05775.1.
IPIIPI00372374.
RefSeqNP_001029315.1.
UniGeneRn.137838

3D structure databases

SMRQ3KRD0. Positions 48-635.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3KRD0.

Proteomic databases

PRIDEQ3KRD0.

Genome annotation databases

EnsemblENSRNOT00000003828; ENSRNOP00000003828; ENSRNOG00000002813; Rattus norvegicus. [Genome view]
GeneID304919.
KEGGrno:304919.
NMPDRfig|10116.3.peg.9359.
UCSCNM_001034143. rat.

Organism-specific databases

CTD304919.
RGD1308286. Dars2.

Phylogenomic databases

eggNOGroNOG07016.
HOVERGENQ3KRD0.
InParanoidQ3KRD0.
OMAPLFEYDE.
OrthoDBEOG91ZHWP.
PhylomeDBQ3KRD0.

Enzyme and pathway databases

BRENDA6.1.1.12. 248.

Gene expression databases

ArrayExpressQ3KRD0.
GenevestigatorQ3KRD0.
GermOnlineENSRNOG00000002813. Rattus norvegicus.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR002312. Asp-tRNA-synth_IIb.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR004115. GAD_dom.
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.
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.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio653833.

Entry information

Entry nameSYDM_RAT
AccessionPrimary (citable) accession number: Q3KRD0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 8, 2005
Last modified: February 9, 2010
This is version 44 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