Skip Header

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

Reviewed, UniProtKB/Swiss-Prot P25151 (SYY2_BACSU)

Last modified February 9, 2010. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Tyrosyl-tRNA synthetase 2
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase 2
      Short name=TyrRS 2
Gene names
Name: tyrS2
Synonyms: tyrR, tyrS1, tyrT, tyrZ
Ordered Locus Names: BSU38460
ORF Names: ipa-9r
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Hide | Top

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

Hide | Top

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. HAMAP MF_02007

Subcellular location

Cytoplasm HAMAP MF_02007.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.

Contains 1 S4 RNA-binding domain.

Hide | Top

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   DomainRepeat
   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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Tyrosyl-tRNA synthetase 2 HAMAP MF_02007
PRO_0000055644

Regions

Repeat89 – 9461 HAMAP MF_02007
Repeat96 – 10162 HAMAP MF_02007
Domain353 – 41361S4 RNA-binding
Region89 – 101132 X 6 AA tandem repeats HAMAP MF_02007
Motif58 – 6710"HIGH" region HAMAP MF_02007
Motif242 – 2465"KMSKS" region HAMAP MF_02007

Sites

Binding site2451ATP By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P25151-1 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 2C6FD6DADEBC33F7

FASTA41347,100
        10         20         30         40         50         60 
MMRTFEQLTA SQQKEVERQL QLYMTGAHEV IPPEELKAKL VKSISTGTPL KIKLGLDPSA 

        70         80         90        100        110        120 
PDVHLGHTVV LNKLRQFQEN GHIVQLLIGD FTGKIGDPTG KSAARKQLTD EEVQHNAKTY 

       130        140        150        160        170        180 
FEQFGKVLDP EKVELHYNSK WLKTLNLEDV IELAGKITVA RLMERDDFEE RIAMQKPISL 

       190        200        210        220        230        240 
HEFFYPLMQG YDSVVLESDI ELGGTDQHFN VLMGRHFQER YNKEKQVVIL MPLLEGLDGV 

       250        260        270        280        290        300 
EKMSKSKHNY IGINEHPNDM YGKTMSLPDS LMKKYIHLAT DLELEEKKQL VKDLETGAVH 

       310        320        330        340        350        360 
PRDAKMLLAR TIVRMYHGEK AAEAAEHSFK TVFQENSLPE DIPAVNWKGE KTIAMIDLLV 

       370        380        390        400        410 
KLKLLSSKSE ARRMIQNGGV RIDGEKVTDV HAKAEIRENM IIQVGKRKFL KLQ

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"A gene encoding a tyrosine tRNA synthetase is located near sacS in Bacillus subtilis."
Glaser P., Kunst F., Debarbouille M., Vertes A., Danchin A., Dedonder R.
DNA Seq. 1:251-261(1991) [PubMed: 1806041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees."
Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.
Mol. Microbiol. 10:371-384(1993) [PubMed: 7934828] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52480 Genomic DNA. Translation: CAA36724.1. Different initiation.
X73124 Genomic DNA. Translation: CAA51565.1.
AL009126 Genomic DNA. Translation: CAB15872.1.
PIRS16426.
RefSeqNP_391725.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID937345.
GenomeReviewsGene locus BSU38460 in contig AL009126_GR.
KEGGbsu:BSU38460.
NMPDRfig|224308.1.peg.3851.

Organism-specific databases

SubtiListBG10555. tyrZ. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMHBG288125.
OMAYVVQVGK.

Enzyme and pathway databases

BRENDA6.1.1.1. 150.

Family and domain databases

HAMAPMF_02007. Tyr_tRNA_synth_type2.
[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...

Hide | Top

Entry information

Entry nameSYY2_BACSU
AccessionPrimary (citable) accession number: P25151
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 16, 2009
Last modified: February 9, 2010
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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