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Reviewed, UniProtKB/Swiss-Prot Q3MEN7 (SYY_ANAVT)

Last modified June 16, 2009. Version 25. 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: Ava_0925
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

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_0000236690

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
Q3MEN7-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 85E4BC864466B926

FASTA39844,447
        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 PDQMLEQYFE LLTDLPIDKL PANPRDRQML LAWEIVKQYH 

       310        320        330        340        350        360 
GEQAAQEAKE AAQSGGKEGA VPEFSLAGVP QFPVKLAYLL GATGLCKSTG EGKRKIQEGG 

       370        380        390 
VRLDGDRISD ADTIFQQPDE LQGRVLQVGK NKFVRLVL 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000117 Genomic DNA. Translation: ABA20549.1.
RefSeqYP_321444.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3681299.
GenomeReviewsGene locus Ava_0925 in contig CP000117_GR.
KEGGava:Ava_0925.
NMPDRfig|240292.3.peg.131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3MEN7.
OMAQ3MEN7. YVVQVGK.

Enzyme and pathway databases

BioCycAVAR240292:AVA_0925-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.
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_ANAVT
AccessionPrimary (citable) accession number: Q3MEN7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 25, 2005
Last modified: June 16, 2009
This is version 25 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