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A1A1W2 (SYY_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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

EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS
Gene names
Name:tyrS
Ordered Locus Names:BAD_0914
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length435 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_02006

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_02006

Subcellular location

Cytoplasm By similarity HAMAP MF_02006.

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: 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 – 435435Tyrosine--tRNA ligase HAMAP MF_02006
PRO_1000088579

Regions

Domain368 – 42558S4 RNA-binding
Motif51 – 6010"HIGH" region HAMAP MF_02006
Motif241 – 2455"KMSKS" region HAMAP MF_02006

Sites

Binding site461Tyrosine By similarity
Binding site1811Tyrosine By similarity
Binding site1851Tyrosine By similarity
Binding site2441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1A1W2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 4AB775F96957D7FA

FASTA43547,968
        10         20         30         40         50         60 
MAHVIDFKEA GFDSVLDELE WRGLISQSTD RDRLAEALNG EPITYYCGFD PTAASLHIGN 

        70         80         90        100        110        120 
LVQLINMRHL QAAGHHPIAL VGGATGLIGD PRQSGERTLN PKDVVAGWAD RLKKQIGGIL 

       130        140        150        160        170        180 
ETEGSNPVRF VSNYDWTASM NVIDFLRDVG KNFRMGTMLA KDTVARRLNS EEGISFTEFS 

       190        200        210        220        230        240 
YQVLQGNDFL HLFDEYHCVL EIGGSDQWGN LTSGLDLIHK VRGVDVNVFT SPIITDAQGK 

       250        260        270        280        290        300 
KFGKSEGNAV WLDGTMLSPY KFYQFWFNRP DSEMENLLKA FTFLPKAEIE RLIEESKTNP 

       310        320        330        340        350        360 
GAREAQRTLA WEVTSFVHGE EATRQAIEAA GALFGRGGDL ADIDESTLEA AIDGMKVDGE 

       370        380        390        400        410        420 
FAKVAAGDRV AEAGMKAGLF KSISEARKTI KSGGVYLNNT RVEDEEQTLQ EGDFLHGRFV 

       430 
LIRRGKKALG VVEQA 

« Hide

References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009256 Genomic DNA. Translation: BAF39695.1.
RefSeqYP_909777.1. NC_008618.1.

3D structure databases

ProteinModelPortalA1A1W2.
SMRA1A1W2. Positions 15-326.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1A1W2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4556733.
GenomeReviewsGene locus BAD_0914 in contig AP009256_GR.
KEGGbad:BAD_0914.
NMPDRfig|1680.3.peg.1184.
PATRIC21101249. VBIBifAdo27973_0988.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
HOGENOMHBG288125.
OMATFYIGFD.
ProtClustDBPRK05912.

Family and domain databases

HAMAPMF_02006. Tyr_tRNA_synth_type1.
[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.
IPR024107. Tyr-tRNA-synth_bac_1.
[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.
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_BIFAA
AccessionPrimary (citable) accession number: A1A1W2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 41 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