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Q6FG10 (SYY_ACIAD) 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:ACIAD0013
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length404 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 – 404404Tyrosine--tRNA ligase HAMAP MF_02007
PRO_0000236688

Regions

Domain342 – 40261S4 RNA-binding
Motif45 – 5410"HIGH" region HAMAP MF_02007
Motif229 – 2335"KMSKS" region HAMAP MF_02007

Sites

Binding site2321ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FG10 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 9B7E696A151BB4E3

FASTA40444,851
        10         20         30         40         50         60 
MSNFLPAEEQ LALIQRGTHE IISEEDLLKK LKENRPLRIK AGFDPTAPDL HLGHTVLINK 

        70         80         90        100        110        120 
LKAFQDLGHE VTFLIGDYTA MIGDPTGKSA TRPPLTREQV EANAKTYQEQ VFKILDPNKT 

       130        140        150        160        170        180 
KVRFNSEWFN QRTAADLIQL ASQQTVSRML ERDDFTKRYN NHQPIAIHEF LYPLVQGYDS 

       190        200        210        220        230        240 
IALEADVELG GTDQTFNLLM GRTLQGRYGQ ESQVCITVPI LEGLDGVNKM SKSLGNYIGV 

       250        260        270        280        290        300 
FDAPGAMYQK VLSMPDTLIE RYFELLSFKS LDEIQGLLDE MANGRNPQDL KKILALELVE 

       310        320        330        340        350        360 
RFHDADAAAN AHKGAGNIIT EGEIPEGTPE VTISRGEFGG EIFIASIVRL AGLTKNAAQA 

       370        380        390        400 
KDAVSRGAVK VDWQVVDANF SVKENKTYLI QAGKKAIAQV TFTD 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG66997.1.
RefSeqYP_044819.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6FG10.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FG10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2880799.
GenomeReviewsGene locus ACIAD0013 in contig CR543861_GR.
KEGGaci:ACIAD0013.
NMPDRfig|62977.3.peg.1079.
PATRIC20738018. VBIAciSp98416_0011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
HOGENOMHBG288125.
OMAYVVQVGK.
PhylomeDBQ6FG10.
ProtClustDBPRK05912.

Enzyme and pathway databases

BioCycASP62977:ACIAD0013-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.
PfamPF00579. 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_ACIAD
AccessionPrimary (citable) accession number: Q6FG10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 19, 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