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Reviewed, UniProtKB/Swiss-Prot Q650K7 (SYY_BACFR)

Last modified November 3, 2009. Version 32. 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: BF0068
OrganismBacteroides fragilis [Complete proteome] [HAMAP]
Taxonomic identifier817 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length430 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 – 430430Tyrosyl-tRNA synthetase HAMAP MF_02006
PRO_0000234678

Regions

Domain362 – 42968S4 RNA-binding
Motif37 – 4610"HIGH" region HAMAP MF_02006
Motif232 – 2365"KMSKS" region HAMAP MF_02006

Sites

Binding site321Tyrosine By similarity
Binding site1721Tyrosine By similarity
Binding site1761Tyrosine By similarity
Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q650K7-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: BCED6F8062160D99

FASTA43048,218
        10         20         30         40         50         60 
MNFVEELRWR GMVHDMMPGT EELLAKEQVT AYVGIDPTAD SLHIGHLCGV MILRHFQRCG 

        70         80         90        100        110        120 
HKPLALIGGA TGMIGDPSGK SAERNLLDEE TLRHNQACIK KQLAKFLDFE SDAPNRAELV 

       130        140        150        160        170        180 
NNYDWMKEFT FLDFAREVGK HITVNYMMAK ESVKKRLNGE ARDGLSFTEF TYQLLQGYDF 

       190        200        210        220        230        240 
LHLYETKGCK LQMGGSDQWG NITTGTELIR RTNGGEAYAL TCPLITKADG GKFGKTESGN 

       250        260        270        280        290        300 
IWLDPRYTSP YKFYQFWLNV SDADAERYIK IFTSLDKAEI DGLVAEHNEA PHLRVLQKRL 

       310        320        330        340        350        360 
AKEVTVMVHS EEDYNAAVDA SNILFGNATS DALKKLDEDT LLAVFEGVPQ FEISRDALVE 

       370        380        390        400        410        420 
GVKAVDLFVD NAAVFASKGE MRKLVQGGGV SLNKEKLAAF DQVITTADLL DEKYLLVQRG 

       430 
KKNYYLIIAK 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

AP006841 Genomic DNA. Translation: BAD46817.1.
RefSeqYP_097351.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3082443.
GenomeReviewsGene locus BF0068 in contig AP006841_GR.
KEGGbfr:BF0068.
NMPDRfig|295405.3.peg.859.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ650K7.
OMATFYIGFD.

Enzyme and pathway databases

BioCycBFRA295405:BF0068-MON.
BRENDA6.1.1.1. 868.

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.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_BACFR
AccessionPrimary (citable) accession number: Q650K7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 32 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