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Q5WEB8 (SYY_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:ABC2758
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length414 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 – 414414Tyrosine--tRNA ligase HAMAP MF_02007
PRO_0000236692

Regions

Domain352 – 41362S4 RNA-binding
Motif57 – 6610"HIGH" region HAMAP MF_02007
Motif241 – 2455"KMSKS" region HAMAP MF_02007

Sites

Binding site2441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WEB8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 384E26C03B8BA7F1

FASTA41447,012
        10         20         30         40         50         60 
MDEKQPLTPE QQKLVDEQVE ALMRGVVEVV PKEAFREKIE KSVRTGKPLN IKLGMDPSAP 

        70         80         90        100        110        120 
DVHIGHTVVL QKLRQFQEYG HHIQLLIGDF TGKIGDPTGK SETRKVLTDE QVKQNAQTYV 

       130        140        150        160        170        180 
EQYGKILDIE KTEILYNSRW LSELKFDDVL KLAGQMTVAR MLEREDFSKR YKTGQPISVH 

       190        200        210        220        230        240 
EFFYPLMQGY DSVAMETDIE VGGTDQTFNL LMGRQLQEAY GKEKQVMLTL PLIEGLDGVR 

       250        260        270        280        290        300 
KMSKSLNNYI GIDEAPNEIF GKAMSIPDEL MVKYYKLATD VPMDEIEALE KGLADGSVHP 

       310        320        330        340        350        360 
RDAKMRLGHK FVEMYHGKEA ADEAEQYFKT VFQKRALPED IPVFSWEGDK EVPLIDLLVT 

       370        380        390        400        410 
LNMQSSKGEA RRMIQGGGVK INEQKITDIH TVVSVEDNMI VQVGKRKFAK LSLT 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD65292.1.
RefSeqYP_176253.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WEB8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WEB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000049335; EBBACP00000048096; EBBACG00000049326.
GeneID3203575.
GenomeReviewsGene locus ABC2758 in contig AP006627_GR.
KEGGbcl:ABC2758.
NMPDRfig|66692.3.peg.2647.
PATRIC18925174. VBIBacCla58185_2937.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
GeneTreeEBGT00050000000599.
HOGENOMHBG288125.
OMAYVVQVGK.
ProtClustDBPRK13354.

Enzyme and pathway databases

BioCycBCLA66692:ABC2758-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.
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_BACSK
AccessionPrimary (citable) accession number: Q5WEB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 48 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