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O13969 (SYTM_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable threonine--tRNA ligase, mitochondrial
EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Gene names
ORF Names:SPAC24C9.09
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processthreonyl-tRNA aminoacylation

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 473Probable threonine--tRNA ligase, mitochondrialPRO_0000035826

Sequences

Sequence LengthMass (Da)Tools
O13969 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 41AE9A95D50967F5

FASTA47354,912
        10         20         30         40         50         60 
MKLKKFQLHT PFAHSCNRVE IYTARFGPTP FSTKANNLKQ PESTLNDHRT IAARQKLYTT 

        70         80         90        100        110        120 
SILTPGSIFF LPHGTRIYNR LVDFLRAQYQ IHGFEEIITP LIFKKDLWEK SGHWQNYEKE 

       130        140        150        160        170        180 
IFRVEESRNV EDEHSNATYG LKPMNCPGHC IVYASTERSY KELPLRFADF SPLHRNEASG 

       190        200        210        220        230        240 
ALSGLTRLRC FHQDDGHIFC SPESIKDEIK NTLTFVKQVY SLLGMNKLKL YLSTRPEEHI 

       250        260        270        280        290        300 
GSLDTWNEAE NGLREALQES GETWIINEGD GAFYGPKIDV MVADARGKWH QTATIQLDFN 

       310        320        330        340        350        360 
LPQRFKLYYR TDAGDNAGSE KLIKQPVMIH RAIFGSLERF MGILIEHLNG HWPFWLSPRH 

       370        380        390        400        410        420 
AVILPVNQTD RILTYAKQVQ KELSNQEVNE SEFLPLNKNT YYVDINAEAQ SIGKRLRESR 

       430        440        450        460        470 
LLNYNYEIVI GEDEVDKEIL SVSSRHNHNS RDTRKMTIQQ LKKEFIENVK AYR

« 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: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB11266.1.
PIRT38350.
RefSeqNP_594034.1. NM_001019459.1.

3D structure databases

ProteinModelPortalO13969.
ModBaseSearch...

Protein-protein interaction databases

STRINGO13969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2541554.
KEGGspo:SPAC24C9.09.
NMPDRfig|4896.1.peg.4004.

Organism-specific databases

GeneDB_SpombeSPAC24C9.09.

Phylogenomic databases

eggNOGfuNOG05978.
GeneTreeEFGT00050000004683.
HOGENOMHBG352811.
OMAWINPRQA.
OrthoDBEOG4RV610.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001662-MONOMER.

Gene expression databases

ArrayExpressO13969.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002320. Thr-tRNA-synth_IIa.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
KOK01868.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
TIGRFAMsTIGR00418. ThrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYTM_SCHPO
AccessionPrimary (citable) accession number: O13969
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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