Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A6KZL8 (SYY_BACV8)

Last modified November 3, 2009. Version 21. 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: BVU_1191
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [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_1000088578

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
A6KZL8-1 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 6CE81313F74A2D79

FASTA43048,041
        10         20         30         40         50         60 
MNFVEELTWR GMVHTMMPGT EELLAKEQVT AYLGIDPTAD SLHIGHLCGV MMLRHFQRCG 

        70         80         90        100        110        120 
HKPLALVGGA TGMIGDPSGK SQERNLLTEE TLRHNVACIK KQLAKFLDFE SDAPNKAELV 

       130        140        150        160        170        180 
NNYDWMKDFT FLDFAREVGK HITVNYMMAK DSVQKRLNGE ARDGLSFTEF TYQLLQGYDF 

       190        200        210        220        230        240 
LHLYETKGCK LQMGGSDQWG NITTGAELIR RTNGGEVFAL TCPLITKADG GKFGKTESGN 

       250        260        270        280        290        300 
IWLDPRYTSP YKFYQFWLNV SDEDAARYIK IFTSLSQEEV EALTAEHAEA PHLRVLQKRL 

       310        320        330        340        350        360 
AKEVTVMVHS EEDYNAAVEA SGILFGNATS EALKKLDEDT LLAVFEGVPQ FEVSRDALAE 

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

       430 
KKNYYLVIAK 

« Hide

References

[1]"Evolution of symbiotic bacteria in the distal human intestine."
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.
PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000139 Genomic DNA. Translation: ABR38882.1.
RefSeqYP_001298504.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6KZL8.

Genome annotation databases

GeneID5302157.
GenomeReviewsGene locus BVU_1191 in contig CP000139_GR.
KEGGbvu:BVU_1191.
NMPDRfig|435590.6.peg.1125.

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.
IPR002942. S4_RNA_bd.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
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_BACV8
AccessionPrimary (citable) accession number: A6KZL8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 24, 2007
Last modified: November 3, 2009
This is version 21 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