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Reviewed, UniProtKB/Swiss-Prot Q5P7U2 (SYY_AZOSE)

Last modified February 9, 2010. Version 35. 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:
    Tyrosyl-tRNA synthetase
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
Gene names
Name: tyrS
Ordered Locus Names: AZOSEA04970
ORF Names: ebA931
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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. HAMAP MF_02007

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02007

Subunit structure

Homodimer By similarity. HAMAP MF_02007

Subcellular location

Cytoplasm By similarity HAMAP MF_02007.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.

Contains 1 S4 RNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtyrosyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Tyrosyl-tRNA synthetase HAMAP MF_02007
PRO_0000236691

Regions

Domain337 – 39862S4 RNA-binding
Motif42 – 5110"HIGH" region HAMAP MF_02007
Motif226 – 2305"KMSKS" region HAMAP MF_02007

Sites

Binding site2291ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P7U2-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: C90C93C4F1F77761

FASTA39944,458
        10         20         30         40         50         60 
MTDVQAALEL IKRGAEELLV EAELVEKLES DRPLRVKAGF DPTAPDLHLG HTVLLNKLRH 

        70         80         90        100        110        120 
FQELGHQVMF LVGDFTAMIG DPSGKNATRP PLSREQILEN ARTYQEQVFK ILDPDKTEIC 

       130        140        150        160        170        180 
FNSSWMESLG TAGMIRLASR YTVARMLERD DFAKRYAGGQ AIAIHEFLYP LCQGYDSVAM 

       190        200        210        220        230        240 
RADVELGGTD QKFNLLVGRE LQKHDRQAPQ CVLMMPLLEG LDGVNKMSKS LGNYIGITEA 

       250        260        270        280        290        300 
PREIFGKIMS ISDSLMWRYF DLLSFHPAVE IARYRAEVEG GRNPRELKVL LAQEIVARFH 

       310        320        330        340        350        360 
SHAAAEDALA DFEARFQRGV LPDDIPEVNV VVGDGGLPVF QVVKQAGLTG STSEALRMIE 

       370        380        390 
QGAVRLNGER VEDKGLVLQR DQTVVLQVGK RKFASVVLN 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI06619.1.
RefSeqYP_157520.1.

3D structure databases

SMRQ5P7U2. Positions 5-399.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P7U2.

Genome annotation databases

GeneID3179684.
GenomeReviewsGene locus AZOSEA04970 in contig CR555306_GR.
KEGGeba:ebA931.
NMPDRfig|76114.4.peg.1430.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
HOGENOMHBG288125.
OMAYVVQVGK.

Enzyme and pathway databases

BioCycASP76114:EBA931-MONOMER.

Family and domain databases

HAMAPMF_02007. Tyr_tRNA_synth_type2.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA_bd.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 1 hit.
PfamPF01479. S4. 1 hit.
PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
SMARTSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_AZOSE
AccessionPrimary (citable) accession number: Q5P7U2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 4, 2005
Last modified: February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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