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Q87LY8 (SYY2_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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 2

EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase 2
Short name=TyrRS 2
Gene names
Name:tyrS2
Ordered Locus Names:VP2470
OrganismVibrio parahaemolyticus [Complete proteome] [HAMAP]
Taxonomic identifier670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length395 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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA 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

Chain1 – 395395Tyrosine--tRNA ligase 2 HAMAP MF_02007
PRO_0000236777

Regions

Domain334 – 39461S4 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
Q87LY8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 078F3A1F77F35C19

FASTA39544,041
        10         20         30         40         50         60 
MASIEAALAE IKRGVEELIP EEELIAKLKE GRPLRIKLGA DPTAPDIHLG HTVIFNKLRL 

        70         80         90        100        110        120 
FQELGHEVTF LIGDFTAMVG DPTGKNTTRP PLSREDVLRN AETYKEQVFK ILDPAKTKIQ 

       130        140        150        160        170        180 
FNSEWLSELG AEGMIRLAAN QTVARMLERD DFKKRYAGGQ PIAIHEFMYP LLQGWDSVAM 

       190        200        210        220        230        240 
ETDVELGGTD QKFNLLMGRE LQKSHGQKPQ VVLMMPLLVG LDGEKKMSKS AGNYIGISEA 

       250        260        270        280        290        300 
PSEMFGKIMS ISDDLMWSYY ELLSFRPLEE IEQFKADVQA GKNPRDIKVL LAKEIIARFH 

       310        320        330        340        350        360 
SEADADAAEQ EFVNRFAKNQ IPDEMPEFDF DAGTPVANLL KDAGLCASTS EAMRMVKQGA 

       370        380        390 
AKVEGEKVAD AKFAPEAGTY VFQVGKRKFA RITIK 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633 / Serotype O3:K6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC60733.1.
RefSeqNP_798849.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87LY8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1189985.
GenomeReviewsGene locus VP2470 in contig BA000031_GR.
KEGGvpa:VP2470.
NMPDRfig|223926.1.peg.2470.
PATRIC20143086. VBIVibPar50997_2370.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG288125.
OMAYVVQVGK.
ProtClustDBPRK05912.

Enzyme and pathway databases

BioCycVPAR223926:VP2470-MONOMER.

Family and domain databases

HAMAPMF_02007. Tyr_tRNA_synth_type2.
[Tree]
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.
IPR024108. Tyr-tRNA-synth_bac_2.
[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.
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 nameSYY2_VIBPA
AccessionPrimary (citable) accession number: Q87LY8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families