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Reviewed, UniProtKB/Swiss-Prot Q81KS9 (SYY1_BACAN)

Last modified November 3, 2009. Version 46. 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 1
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase 1
      Short name=TyrRS 1
Gene names
Name: tyrS1
Synonyms: tyrS-1
Ordered Locus Names: BA_4911, GBAA_4911, BAS4556
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length418 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 By similarity.

Subcellular location

Cytoplasm By similarity.

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
   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 – 418418Tyrosyl-tRNA synthetase 1 HAMAP MF_02006
PRO_0000234667

Regions

Domain352 – 41867S4 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
Q81KS9-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6D95DA9182AAC32A

FASTA41847,035
        10         20         30         40         50         60 
MGILQDLEFR GLINQQTDAE GLEQLLEKES VKLYCGFDPT ADSLHIGHML PVLMLRRFQL 

        70         80         90        100        110        120 
AGHQPIALVG GGTGMIGDPS GKKAERTLNT KDTVAYYTES IKNQLSNFLE FENVENPATM 

       130        140        150        160        170        180 
ANNYDWLGNL DVISFLRDIG KNFGLNYMLA KDTVASRLET GISFTEFSYM ILQSYDFLNL 

       190        200        210        220        230        240 
YQHHNCRLQI GGSDQWGNIT AGLELIRKSE EDAKAFGLTI PLVTKSDGTK FGKTEGGAIW 

       250        260        270        280        290        300 
LDPEKTTPYE FYQFWINTDD RDVVKYLKYF TFLSHEEILE LEKQVAEAPE KRAAQKALGA 

       310        320        330        340        350        360 
EMTKLVHGEE ALEQAIKISA ALFSGSVAEL TASEIEQGFK DVPSVERTAE DTVLIDLLVE 

       370        380        390        400        410 
SKISPSKRQA REDVTNGAIY VNGERTQALD YVVTEKDRIE GKFTIIRRGK KKYFLIRY 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP28595.1.
AE017334 Genomic DNA. Translation: AAT34029.1.
AE017225 Genomic DNA. Translation: AAT56853.1.
RefSeqNP_847109.1.
YP_021554.1.
YP_030803.1.

3D structure databases

HSSPHSSP built from PDB template 2TS1 based on UniProtKB P00952.
SMRQ81KS9. Positions 1-319.
ModBaseSearch...

Genome annotation databases

GeneID1084086.
2818653.
2850360.
GenomeReviewsGene locus BA_4911 in contig AE016879_GR.
Gene locus BAS4556 in contig AE017225_GR.
Gene locus GBAA_4911 in contig AE017334_GR.
KEGGban:BA4911.
bar:GBAA4911.
bat:BAS4556.
TIGRBA_4911.
GBAA_4911.

Phylogenomic databases

HOGENOMQ81KS9.
OMAPGYVPNT.

Enzyme and pathway databases

BioCycBANT260799:BAS4556-MON.
BANT261594:GBAA4911-MON.
BRENDA6.1.1.1. 267517.

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 nameSYY1_BACAN
AccessionPrimary (citable) accession number: Q81KS9
Secondary accession number(s): Q6HS85, Q6KLI4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 46 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