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Q6MNQ2 (SYY_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:Bd1189
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio

Protein attributes

Sequence length405 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 – 405405Tyrosine--tRNA ligase HAMAP MF_02007
PRO_0000236695

Regions

Domain341 – 40464S4 RNA-binding
Motif46 – 5510"HIGH" region HAMAP MF_02007
Motif230 – 2345"KMSKS" region HAMAP MF_02007

Sites

Binding site2331ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MNQ2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 00B1E7BC51690858

FASTA40545,368
        10         20         30         40         50         60 
MMSPQEQLER IKFGTADFIN DEDMLKKLKR SIETKKPLNI KLGADPTRPD IHLGHTVVIN 

        70         80         90        100        110        120 
KLKTFQDLGH KVSFLIGDFT AMIGDPSGKN STRPMLTREE IEENGRSYAK QIFKILDPEK 

       130        140        150        160        170        180 
TEIVYNSSWI MKMTPAEFIT MTSKYTVAQL LEREDFTKRY RSGTPIGIHE FIYPLTQGYD 

       190        200        210        220        230        240 
SVALKTDVEL GGTDQKFNLL VGRAMQAAYG MEAQCVLTMP ILEGIDGVNK MSKSLDNYIS 

       250        260        270        280        290        300 
VVDTPKDMFG KTMRISDELM YRWYELLTDV GAAGLNQLRA DVAEGRKHPR TVKVELAKFL 

       310        320        330        340        350        360 
IKRFHSQAEA QAAEDEFNRI FVEKGLPDEV PDFEVEAETQ MGLAALMVKA QLAASNSEAG 

       370        380        390        400 
RLIQGGGVQI DGEKVSDPRL KIDLKSGASF VLKAGKKKFV KIVVK 

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842649 Genomic DNA. Translation: CAE79099.1.
RefSeqNP_968106.1. NC_005363.1.

3D structure databases

ProteinModelPortalQ6MNQ2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2733227.
GenomeReviewsGene locus Bd1189 in contig BX842601_GR.
KEGGbba:Bd1189.
NMPDRfig|264462.1.peg.1076.
PATRIC21076990. VBIBdeBac73187_1076.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG288125.
OMAYVVQVGK.
PhylomeDBQ6MNQ2.
ProtClustDBPRK05912.

Enzyme and pathway databases

BioCycBBAC264462:BD1189-MONOMER.

Family and domain databases

HAMAPMF_02007. Tyr_tRNA_synth_type2.
[Tree]
InterProIPR002305. 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. False negative.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_BDEBA
AccessionPrimary (citable) accession number: Q6MNQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 50 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