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Reviewed, UniProtKB/Swiss-Prot A7Z7R1 (SYY_BACA2)

Last modified November 3, 2009. Version 16. 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: RBAM_026790
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02006

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 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 – 421421Tyrosyl-tRNA synthetase HAMAP MF_02006
PRO_1000088576

Regions

Domain355 – 42167S4 RNA-binding
Motif40 – 4910"HIGH" region HAMAP MF_02006
Motif232 – 2365"KMSKS" region HAMAP MF_02006

Sites

Binding site351Tyrosine By similarity
Binding site1701Tyrosine By similarity
Binding site1741Tyrosine By similarity
Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z7R1-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 86BF61436EA25779

FASTA42147,756
        10         20         30         40         50         60 
MTNLLEDLSF RGLIQQMTDE EGLNKQLNEE KIRLYSGFDP TADSLHIGHL LPILTLRRFQ 

        70         80         90        100        110        120 
LAGHHPIALV GGATGLIGDP SGKKAERTLN TQDIVVEWSQ KIKNQLSRFL DFEAGENPAV 

       130        140        150        160        170        180 
IANNFDWIGK LSIIEFLRDV GKNFGINYML AKDTVSSRIE TGISYTEFSY MILQSYDFLN 

       190        200        210        220        230        240 
LYREKNCKLQ IGGSDQWGNI TAGLELIRKS EEEGAKAFGL TIPLVTKADG TKFGKTEGGA 

       250        260        270        280        290        300 
IWLDKEKTSP YEFYQFWINT DDRDVVKYLK YFTFLSKEEI EAYAEKTETA PEKREAQKRL 

       310        320        330        340        350        360 
AEEVTVLVHG REALEQAVHI SQALFSGNIK ELSAQDVKVG FKDVPSFEKD RSEELSLVDV 

       370        380        390        400        410        420 
LVESKLSPSK RQAREDIQNG AVYINGERQT DIGHLLTAED RIEDQFTVLR RGKKKYFLIT 


Y 

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References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000560 Genomic DNA. Translation: ABS75037.1.
RefSeqYP_001422268.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7Z7R1.

Genome annotation databases

GeneID5460229.
GenomeReviewsGene locus RBAM_026790 in contig CP000560_GR.
KEGGbay:RBAM_026790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMATFYIGFD.

Family and domain databases

HAMAPMF_02006.
[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_BACA2
AccessionPrimary (citable) accession number: A7Z7R1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 16 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