Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q2NJG7 (SYY_AYWBP)

Last modified September 1, 2009. Version 23. 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: AYWB_309
OrganismAster yellows witches'-broom phytoplasma (strain AYWB) [Complete proteome] [HAMAP]
Taxonomic identifier322098 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeCandidatus PhytoplasmaCandidatus Phytoplasma asteris

Protein attributes

Sequence length413 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 – 413413Tyrosyl-tRNA synthetase HAMAP MF_02006
PRO_0000234666

Regions

Domain347 – 41367S4 RNA-binding
Motif39 – 4810"HIGH" region HAMAP MF_02006
Motif225 – 2295"KMSKS" region HAMAP MF_02006

Sites

Binding site341Tyrosine By similarity
Binding site1641Tyrosine By similarity
Binding site1681Tyrosine By similarity
Binding site2281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2NJG7-1 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: C8C3BEA5A2B0A12F

FASTA41347,600
        10         20         30         40         50         60 
MSFYEELKWR NLIKDCNNEI QVKELLDNNQ VKFYCGFDPT SHSLTVGHLI QITMILLMQR 

        70         80         90        100        110        120 
QGHLPVILVG GATGLIGDPK ETEERKLLSL ENSLQNAKSI ESQLKTILLN KQVEFVNNYQ 

       130        140        150        160        170        180 
WLSQIDIISF LRNYGKFFNI NYMLSKHVVA KRLASGISFT EFSYMILQSL DFHHLYKNHK 

       190        200        210        220        230        240 
VRLQLGGSDQ WGNITSGLEI IRKLEKKSDA LGVSTPLLLN SDGTKFGKSE KRVLWLNPLM 

       250        260        270        280        290        300 
TSPYEIYQYF LNVSDKEVIN YLKMLTLIPK KGILELEKKT LENPQKRLAQ KALTQSIINL 

       310        320        330        340        350        360 
IHSSDILQEC IKTNQILFSN AKKESFQEKD FILLQKTLFC HSIKEDILLV DALVQTKLAT 

       370        380        390        400        410 
SKSEAREFIK DNTIKLFNQK IKSLDFIITK ENTLFGKYIL LKKGKKNNAL IVF 

« Hide

References

[1]"Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hosts."
Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.
J. Bacteriol. 188:3682-3696(2006) [PubMed: 16672622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000061 Genomic DNA. Translation: ABC65426.1. Different initiation.
RefSeqYP_456505.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2NJG7.

Genome annotation databases

GeneID3865903.
GenomeReviewsGene locus AYWB_309 in contig CP000061_GR.
KEGGayw:AYWB_309.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2NJG7.

Family and domain databases

HAMAPMF_02006.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA_bd.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
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. False negative.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_AYWBP
AccessionPrimary (citable) accession number: Q2NJG7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: September 1, 2009
This is version 23 of the entry and version 2 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