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Q65MW0 (SYY2_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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 2

EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase 2
Short name=TyrRS 2
Gene names
Name:tyrS2
Ordered Locus Names:BLi00666, BL00484
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length417 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 – 417417Tyrosine--tRNA ligase 2 HAMAP MF_02007
PRO_0000236694

Regions

Domain354 – 41562S4 RNA-binding
Motif59 – 6810"HIGH" region HAMAP MF_02007
Motif243 – 2475"KMSKS" region HAMAP MF_02007

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65MW0 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 70CEA3B806D32AF7

FASTA41747,192
        10         20         30         40         50         60 
MQQQQFDQLT TAEKREVERQ LHLYMDGAEE VIPPEELRAK LAKSILTGEP LKIKLGLDPS 

        70         80         90        100        110        120 
APDVHLGHTV VLNKLRQFQE NGHIVQLLIG DFTGKIGDPT GKSAARKQLT DEEVRRNAET 

       130        140        150        160        170        180 
YFQQFGKVLD QNKVELHYNS KWLKRLTLED VIELAGKITV ARLMERDDFE ERIAMQKPIS 

       190        200        210        220        230        240 
LHEFFYPLMQ GYDSVVLDSD IELGGTDQHF NVLMGRHFQE KYGKEKQVVI LMPLLEGLDG 

       250        260        270        280        290        300 
IEKMSKSKNN YIGIDEDPHE MFGKTMSLPD SLMKKYIHLA TDLEAEEKKR LVKDLETGAV 

       310        320        330        340        350        360 
HPRDAKMLLG KTIVNMYHGS KAAEAAEQQF KKVFQQNSAP DNITAVHWQG GGTVPVTDLL 

       370        380        390        400        410 
VTLELLPSKS EARRMIQNGG VKINGAKAES IHADIALEHG MIIQVGKRKF VKLQMHQ 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU39604.1.
CP000002 Genomic DNA. Translation: AAU22255.1.
RefSeqYP_077893.1. NC_006270.3.
YP_090297.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65MW0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65MW0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000054858; EBBACP00000053389; EBBACG00000054849.
EBBACT00000059664; EBBACP00000058097; EBBACG00000059655.
GeneID3031036.
3100653.
GenomeReviewsGene locus BLi00666 in contig AE017333_GR.
Gene locus BL00484 in contig CP000002_GR.
KEGGbld:BLi00666.
bli:BL00484.
NMPDRfig|279010.5.peg.925.
PATRIC18946853. VBIBacLic203714_0651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
GeneTreeEBGT00050000000599.
HOGENOMHBG288125.
OMAYVVQVGK.
PhylomeDBQ65MW0.
ProtClustDBPRK13354.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI00666-MONOMER.
BLIC279010:BL00484-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.
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 nameSYY2_BACLD
AccessionPrimary (citable) accession number: Q65MW0
Secondary accession number(s): Q62YA3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 56 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