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Q5I0L3 (SYYM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. 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:
Tyrosine--tRNA ligase, mitochondrial

EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS
Gene names
Name:Yars2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity.

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtyrosyl-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

tyrosine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 471Tyrosine--tRNA ligase, mitochondrialPRO_0000250721

Regions

Motif76 – 8510"HIGH" region
Motif275 – 2795"KMSKS" region

Sites

Binding site2781ATP By similarity

Amino acid modifications

Modified residue3491N6-acetyllysine By similarity
Modified residue4201Phosphotyrosine By similarity
Modified residue4291Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5I0L3 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: A9431FD9EA3FBE92

FASTA47152,628
        10         20         30         40         50         60 
MAAPMLRHLC RVPQSGVWTR GPRAVRPGAR GMLVAPRARG LFKEFFPESG TKTELPELFD 

        70         80         90        100        110        120 
RRRAGSPQTV YCGFDPTGDS LHVGHLLTLL GLFHFQRAGH NVIALVGGST ALLGDPSGRT 

       130        140        150        160        170        180 
KEREALSAEC VRANARALQR GLETLAANHA RLFADGRPWG TFTVLDNAAW FQKQHLMDFL 

       190        200        210        220        230        240 
ATVGGHFRMG TLLSRLSVQS RLKSPEGMSL AEFFYQVLQA YDFYYLFRHY GCRVQLGGSD 

       250        260        270        280        290        300 
QLGNIMSGYE FIHKLTGEDV FGITVPLITS TTGAKLGKSA GNAVWLNREK TSPFELYQFF 

       310        320        330        340        350        360 
IRQQDDSVER YLKLFTFLPL PEIDHIMQLH VKEPEKRIAQ KRLAAEVTKL VHGQEGLDSA 

       370        380        390        400        410        420 
KRCTQALYHS SIEALEVMSD QELKELFKEA SFSELVLDPG TSVIDTCRKA NAIPDGPRGY 

       430        440        450        460        470 
RMITEGGVSI NHRQVTNPES VLVIGQHILK NGLSLLKIGK RNFYIIKWLQ L 

« 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: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC088224 mRNA. Translation: AAH88224.1.
IPIIPI00370436.
RefSeqNP_001009627.1. NM_001009627.1.
UniGeneRn.163187.

3D structure databases

HSSPHSSP built from PDB template 4TS1 based on UniProtKB P00952.
ProteinModelPortalQ5I0L3.
SMRQ5I0L3. Positions 31-367.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5I0L3.

Proteomic databases

PRIDEQ5I0L3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000034902; ENSRNOP00000037398; ENSRNOG00000025252.
GeneID287924.
KEGGrno:287924.
NMPDRfig|10116.3.peg.7839.
UCSCNM_001009627. rat.

Organism-specific databases

CTD51067.
RGD1311696. Yars2.

Phylogenomic databases

eggNOGroNOG05666.
GeneTreeENSGT00390000013709.
HOVERGENHBG056052.
InParanoidQ5I0L3.
OMALVHGQEG.
OrthoDBEOG47H5Q1.
PhylomeDBQ5I0L3.

Gene expression databases

ArrayExpressQ5I0L3.
GenevestigatorQ5I0L3.
GermOnlineENSRNOG00000025252. Rattus norvegicus.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-synth.
IPR024088. Tyr-tRNA-synth_bac-type.
[Graphical view]
Gene3DG3DSA:3.10.290.10. G3DSA:3.10.290.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01866.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. TyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio627220.

Entry information

Entry nameSYYM_RAT
AccessionPrimary (citable) accession number: Q5I0L3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 58 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