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P67611 (SYY_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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
EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS
Gene names
Name:tyrS
Ordered Locus Names:Rv1689, MT1728
ORF Names:MTCI125.11
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-Rule MF_02006

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP-Rule MF_02006

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

Was identified as a high-confidence drug target. HAMAP-Rule MF_02006

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.

Contains 1 S4 RNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Tyrosine--tRNA ligase HAMAP-Rule MF_02006
PRO_0000055660

Regions

Domain356 – 41358S4 RNA-binding
Motif41 – 5010"HIGH" region HAMAP-Rule MF_02006
Motif231 – 2355"KMSKS" region HAMAP-Rule MF_02006

Sites

Binding site361Tyrosine By similarity
Binding site1711Tyrosine By similarity
Binding site1751Tyrosine By similarity
Binding site2341ATP By similarity

Secondary structure

1 ................................................................................. 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P67611 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: A8DAFEC1085CB491

FASTA42446,330
        10         20         30         40         50         60 
MSGMILDELS WRGLIAQSTD LDTLAAEAQR GPMTVYAGFD PTAPSLHAGH LVPLLTLRRF 

        70         80         90        100        110        120 
QRAGHRPIVL AGGATGMIGD PRDVGERSLN EADTVAEWTE RIRGQLERFV DFDDSPMGAI 

       130        140        150        160        170        180 
VENNLEWTGS LSAIEFLRDI GKHFSVNVML ARDTIRRRLA GEGISYTEFS YLLLQANDYV 

       190        200        210        220        230        240 
ELHRRHGCTL QIGGADQWGN IIAGVRLVRQ KLGATVHALT VPLVTAADGT KFGKSTGGGS 

       250        260        270        280        290        300 
LWLDPQMTSP YAWYQYFVNT ADADVIRYLR WFTFLSADEL AELEQATAQR PQQRAAQRRL 

       310        320        330        340        350        360 
ASELTVLVHG EAATAAVEHA SRALFGRGEL ARLDEATLAA ALRETTVAEL KPGSPDGIVD 

       370        380        390        400        410        420 
LLVASGLSAS KGAARRTIHE GGVSVNNIRV DNEEWVPQSS DFLHGRWLVL RRGKRSIAGV 


ERIG

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842577 Genomic DNA. Translation: CAB10946.1.
AE000516 Genomic DNA. Translation: AAK45997.1.
AL123456 Genomic DNA. Translation: CCP44454.1.
PIRH70501.
RefSeqNP_216205.1. NC_000962.3.
NP_336183.1. NC_002755.2.
YP_006515081.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JANX-ray2.90A/B/C/D1-424[»]
ProteinModelPortalP67611.
SMRP67611. Positions 5-423.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv1689.

Proteomic databases

PRIDEP67611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK45997; AAK45997; MT1728.
GeneID13316471.
885668.
923980.
KEGGmtc:MT1728.
mtu:Rv1689.
mtv:RVBD_1689.
PATRIC18125554. VBIMycTub22151_1891.

Organism-specific databases

TubercuListRv1689.

Phylogenomic databases

eggNOGCOG0162.
HOGENOMHOG000242790.
KOK01866.
OMAGKKKHVL.
ProtClustDBPRK05912.

Family and domain databases

Gene3D3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_02006. Tyr_tRNA_synth_type1.
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-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
IPR024107. Tyr-tRNA-ligase_bac_1.
[Graphical view]
PANTHERPTHR11766. PTHR11766. 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. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP67611.

Entry information

Entry nameSYY_MYCTU
AccessionPrimary (citable) accession number: P67611
Secondary accession number(s): L0TA47, O33191
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 59 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

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents