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P28669 (SYYM_PODAS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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:YTS1
OrganismPodospora anserina (Pleurage anserina)
Taxonomic identifier5145 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Has both an aminoacyl-tRNA synthetase activity and is involved in the splicing of group I introns.

Catalytic activity

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

Subcellular location

Mitochondrion matrix.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
mRNA processing
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosyl-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? – 640Tyrosine--tRNA ligase, mitochondrialPRO_0000035834

Regions

Motif105 – 11410"HIGH" region
Motif322 – 3265"KMSKS" region

Sites

Binding site3251ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P28669 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 1DBA1C469FF5E3C6

FASTA64072,406
        10         20         30         40         50         60 
MSMSRGSVCR RCLLTMKSMA GGGPTSTYAQ QRGKKTWHGP KYQAKIDQAQ ADWEERAEKI 

        70         80         90        100        110        120 
KKGEIQHTWD MFVERGYVKD TAGSHETIRK LMLHKRIGAY TGIDPTAPSL HIGHLLPLMP 

       130        140        150        160        170        180 
IFWMYMHGYA GYTLIGGATA KIGDPTDRLV SRTPLKRTDL TMNLTKIHYQ LKALWMNVEE 

       190        200        210        220        230        240 
QARRRGFEKD WAWKRAVVNN STWWNSLPLI EVLKRLGDSM RMGPLLSRDT VKNKMSKGDG 

       250        260        270        280        290        300 
MSFSEFTYPL MQGWDWWHMY QANGIQMQIG GSDQYGNIVT GVETVKVVRD NEPDPAKKIE 

       310        320        330        340        350        360 
GGPFNDPVGF TVPLLTDSAG VKFGKSAGNA FLDKFQTSEF DLYGYFVRRS DQEVEKLLKL 

       370        380        390        400        410        420 
FTFLPMENIN EAMKIHSENP ARRVAQHLLA FEVVGLVHGM NAAHRTALNH QARYGKQIDI 

       430        440        450        460        470        480 
PGVTLRMPKA ATEDTPPSIL DAPKMDMQLP ESLIMGKSIG RILYAAGLAK SASEGHRLAT 

       490        500        510        520        530        540 
QQGAYIGAMP GHKRTEDNKV MDYSQLSFTP IKLWFPQETR NYLIDGKLLI LRKGKVQIRV 

       550        560        570        580        590        600 
IEMVSDEEWK ESGQTYPGEP GTGALRMLRQ QLKMLKSGML TPDEVKANLK NHVEEEAPPP 

       610        620        630        640 
GFMKFPDQDS YAIRRATQEL MDEIHQKEVG GDSPREERRE 

« Hide

References

[1]"The mitochondrial tyrosyl-tRNA synthetase of Podospora anserina is a bifunctional enzyme active in protein synthesis and RNA splicing."
Kaempfer U., Kueck U., Cherniak A.D., Lambowitz A.M.
Mol. Cell. Biol. 12:499-511(1992) [PubMed: 1531084] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: s.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54981 Genomic DNA. Translation: CAA38725.1.
PIRA42019.

3D structure databases

ProteinModelPortalP28669.
SMRP28669. Positions 40-414.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-synth.
IPR024088. Tyr-tRNA-synth_bac-type.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
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...

Entry information

Entry nameSYYM_PODAS
AccessionPrimary (citable) accession number: P28669
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families