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Reviewed, UniProtKB/Swiss-Prot Q8YSU9 (SYY_ANASP)

Last modified November 3, 2009. Version 40. 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: alr2982
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length398 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_02007

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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: 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 – 398398Tyrosyl-tRNA synthetase HAMAP MF_02007
PRO_0000236689

Regions

Domain334 – 39865S4 RNA-binding
Motif48 – 5710"HIGH" region HAMAP MF_02007
Motif235 – 2395"KMSKS" region HAMAP MF_02007

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YSU9-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D5E177EDE434A4FA

FASTA39844,439
        10         20         30         40         50         60 
MAENFSWLHR GIAEVFPQPT DAESDIESLE KRLATTDRPL RVKYGIDPTG ADIHLGHSIP 

        70         80         90        100        110        120 
MRKLRGFQDA GHTAVLIIGD FTARIGDPTG KSEMRRQLTE EDVKQNAQTY LDQVRPILDF 

       130        140        150        160        170        180 
DTPGRLEVRY NSEWLSRLDL GKITELLATM TVGQMLAKEG FADRYKKENP IFLHEFLYPL 

       190        200        210        220        230        240 
MQGYDSVAIE ADVELGGTDQ KFNIAVGRDL QRHFGQKPQF GVLLPILIGT DGVQKMSKSL 

       250        260        270        280        290        300 
GNYVSLSEHP GQKYQKLQGV PDVLLKDYFE LLTNLPIDAL PENPRDRQML LAWEIVKQYH 

       310        320        330        340        350        360 
GEQAANEAKE AAQSGGKEGA VPEFSLSNVS QFPVKLAYLL GATGLCKSTG EGKRKIQEGG 

       370        380        390 
VRLDGDRISD ADTTFQQPDE LQGRVLQVGK NKFMRLVP 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000019 Genomic DNA. Translation: BAB74681.1.
PIRAG2178.
RefSeqNP_487022.1.

3D structure databases

HSSPHSSP built from PDB template 1H3F based on UniProtKB P83453.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YSU9.

Genome annotation databases

GeneID1106580.
GenomeReviewsGene locus alr2982 in contig BA000019_GR.
KEGGana:alr2982.
NMPDRfig|103690.1.peg.3289.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8YSU9.
OMAYVVQVGK.

Enzyme and pathway databases

BioCycNSP103690:ALR2982-MON.

Family and domain databases

HAMAPMF_02007.
[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.
PfamPF01479. S4. 1 hit.
PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_ANASP
AccessionPrimary (citable) accession number: Q8YSU9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2002
Last modified: November 3, 2009
This is version 40 of the entry and version 1 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