Skip Header

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

Reviewed, UniProtKB/Swiss-Prot P04077 (SYY_BACCA)

Last modified June 16, 2009. Version 69. 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
OrganismBacillus caldotenax
Taxonomic identifier1395 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length419 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. HAMAP MF_02006

Subcellular location

Cytoplasm. HAMAP MF_02006

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
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 – 419419Tyrosyl-tRNA synthetase HAMAP MF_02006
PRO_0000055641

Regions

Domain352 – 41968S4 RNA-binding
Motif39 – 4810"HIGH" region HAMAP MF_02006
Motif230 – 2345"KMSKS" region HAMAP MF_02006

Sites

Binding site341Tyrosine By similarity
Binding site1691Tyrosine By similarity
Binding site1731Tyrosine By similarity
Binding site2331ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P04077-1 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 13785CC4FBFEB742

FASTA41947,202
        10         20         30         40         50         60 
MDLLAELQWR GLVNQTTDED GLRKLLNEER VTLYCGFDPT ADSLHIGNLA AILTLRRFQQ 

        70         80         90        100        110        120 
AGHRPIALVG GATGLIGDPS GKKSERTLNA KETVEAWSAR IKEQLGRFLD FEADGNPAKI 

       130        140        150        160        170        180 
KNNYDWIGPL DVITFLRDVG KHFSVNYMMA KESVQSRIET GISFTEFSYM MLQAYDFLRL 

       190        200        210        220        230        240 
YETEGCRLQI GGSDQWGNIT AGLELIRKTK GEARAFGLTI PLVTKADGTK FGKTESGTIW 

       250        260        270        280        290        300 
LDKEKTSPYE FYQFWINTDD RDVIRYLKYF TFLSKEEIEA LEQELREAPE KRAAQKALAE 

       310        320        330        340        350        360 
EVTKLVHGEE ALRQAIRISE ALFSGDIANL TAAEIEQGFK DVPSFVHEGG DVPLVELLVS 

       370        380        390        400        410 
AGISPSKRQA REDIQNGAIY VNGERLQDVG AILTAEHRLE GRFTVIRRGK KKYYLIRYA 

« Hide

References

[1]"Natural variation of tyrosyl-tRNA synthetase and comparison with engineered mutants."
Jones M.D., Lowe D.M., Borgford T., Fersht A.R.
Biochemistry 25:1887-1891(1986) [PubMed: 3011073] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

M13148 Genomic DNA. Translation: AAA22877.1.
PIRSYBSYX. A01180.

3D structure databases

HSSPHSSP built from PDB template 1JH3 based on UniProtKB P00952.
SMRP04077. Positions 1-319, 321-419.
ModBaseSearch...

Enzyme and pathway databases

BRENDA6.1.1.1. 1001.

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.
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_BACCA
AccessionPrimary (citable) accession number: P04077
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: June 16, 2009
This is version 69 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