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Reviewed, UniProtKB/Swiss-Prot O74890 (SYYM_SCHPO)

Last modified November 3, 2009. Version 56. 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

Names and origin

Protein namesRecommended name:
    Tyrosyl-tRNA synthetase, mitochondrial
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
Gene names
Name: msy1
ORF Names: SPCC576.06c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). UniProtKB P48527

Subcellular location

Mitochondrion matrix. Ref.2 UniProtKB P48527

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Contains 1 S4 RNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   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 componentmitochondrial matrix

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

Transit peptide1 – ?Mitochondrion Potential UniProtKB P48527
Chain? – 445Tyrosyl-tRNA synthetase, mitochondrial UniProtKB P48527PRO_0000314632

Regions

Domain384 – 44562S4 RNA-binding
Motif38 – 4710"HIGH" region
Motif245 – 2495"KMSKS" region

Sites

Binding site2481ATP By similarity UniProtKB P83453

Sequences

Sequence LengthMass (Da)Tools
O74890-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E47BD594369C7EE2

FASTA44549,498
        10         20         30         40         50         60 
MSRLLACLKQ LQARSLIHNT TLLQPSCNVN SVYLGADPTA ASLHVGNLVA LMPLVHFFLN 

        70         80         90        100        110        120 
GFPVFTVIGD ATAQLGDPSG RSTSRKQMAE TTRTANSNSI HNQLKDLSSS ILSYAQDCNY 

       130        140        150        160        170        180 
PFSQMPSSSQ WSIVRNSSWY ENLKLLKFLS SVGPHVRVSQ MLARDSVTTR LQSPSGLSFA 

       190        200        210        220        230        240 
ELTYQLLQAY DYSYLYENHS VNLQIGGSDQ WGNITAGTDL VRRTHPNANV YALTTPLLTS 

       250        260        270        280        290        300 
SSGQKLGKSA GNAIWLDPKL TDSYSLYQYF ISAPDDLACK CLDMLTLLPL EQLEQIKAEH 

       310        320        330        340        350        360 
EKDPSQRIVH KYLASNVVRM VHGKKALELA QIQTKLLHGA HQAPFGFYSE APQQGDSFPS 

       370        380        390        400        410        420 
LPEIRALFKD CKFYRTIDSS IKDQPFSRLL RTLQIYTSRK EATEHILSGA VSLGHKPILD 

       430        440 
SNYKFPDNSL FVLRAGKRTF VLDSL 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

CU329672 Genomic DNA. Translation: CAA21185.1.
PIRT41416.
RefSeqNP_588433.1.

3D structure databases

HSSPHSSP built from PDB template 1TYA based on UniProtKB P00952.
ModBaseSearch...

Protein-protein interaction databases

STRINGO74890.

Genome annotation databases

GeneID2539529.
GenomeReviewsGene locus msy1 in contig CU329672_GR.
KEGGspo:SPCC576.06c.
NMPDRfig|4896.1.peg.771.

Organism-specific databases

GeneDB_SpombeSPCC576.06c.

Phylogenomic databases

OMAISLYCGV.

Enzyme and pathway databases

BRENDA6.1.1.1. 653.

Gene expression databases

ArrayExpressO74890.

Family and domain databases

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.
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...

Entry information

Entry nameSYYM_SCHPO
AccessionPrimary (citable) accession number: O74890
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 1, 1998
Last modified: November 3, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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