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Reviewed, UniProtKB/Swiss-Prot Q3UQ84 (SYTM_MOUSE)

Last modified June 16, 2009. Version 34. 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:
    Threonyl-tRNA synthetase, mitochondrial
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS
    Threonyl-tRNA synthetase-like 1
Gene names
Name: Tars2
Synonyms: Tarsl1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length723 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
Gene Ontology (GO)
   Biological processthreonyl-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

threonine-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
Chain? – 723Threonyl-tRNA synthetase, mitochondrialPRO_0000254587

Experimental info

Sequence conflict91R → G in BAB27683. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3UQ84-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 046BF1D524D1EDCA

FASTA72381,700
        10         20         30         40         50         60 
MGLCLRWRRL GFPLPEFRRC ELHTVREASA PTPPHWLAER FGLFEELWTA HVKKLASMTQ 

        70         80         90        100        110        120 
KKARAIKISL PEGQKVDAVA WNTTPYQLAH QISVTLADTA VAAEVNGELY DLDRPLETDC 

       130        140        150        160        170        180 
HLRFLTFDSP EGKAVFWHSS AHVLGAAAEQ QLGAVLCRGP STESGFYHDF FLGKERTVRS 

       190        200        210        220        230        240 
AELPILERIC QELIAAAQPF RRLEASRDQL RQLFKDNHFK LHLIEEKVTG PTATVYGCGM 

       250        260        270        280        290        300 
SVDLCRGPHL RHTGQIGALK LLTNSSALWR SLGAPETLQR VSGISFPKVE LLRNWEARRE 

       310        320        330        340        350        360 
AAELRDHRRI GKEQELFFFH ELSPGSCFFL PRGTRVYNAL VAFIRAEYAR RGFSEVKTPT 

       370        380        390        400        410        420 
LFSTKLWEQS GHWEHYRADM FSLKPPGTDG VDNSQSGHPA RCPKDTLALK PMNCPAHCLM 

       430        440        450        460        470        480 
FAHRPRSWRE LPVRLADFGA LHRAEASGSL GGLTRLWRFQ QDDAHIFCAP HQLEAEIQGC 

       490        500        510        520        530        540 
LDFLRCVYSV LGFSFHLALS TRPPGFLGEP RLWDQAEQVL QQALEKFGEP WDLNPGDGAF 

       550        560        570        580        590        600 
YGPKIDVHLH DALGRPHQCG TIQLDFQLPL RFDLQYKGPA GTPECPVLIH RAVLGSVERL 

       610        620        630        640        650        660 
LGVLAESCGG KWPLWLSPLQ VVVIPVRTEQ EEYARQVQQC LQAAGLVSDL DADSGLTLSR 

       670        680        690        700        710        720 
RVRRAQLAHY NFQFVVGQRE QSQRTVNVRT RDNRQLGERD LAESVQRLLE LQNARVPNAE 


EVF 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.

Cross-references

Sequence databases

AK142685 mRNA. Translation: BAE25159.1.
AK011540 mRNA. Translation: BAB27683.1.
IPIIPI00132419.
RefSeqNP_082207.1.
UniGeneMm.271754

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000028107. Mus musculus. [Contig view]
GeneID71807.
KEGGmmu:71807.
NMPDRfig|10090.3.peg.8581.

Organism-specific databases

MGIMGI:1919057. Tars2.

Phylogenomic databases

HOVERGENQ3UQ84.
OMAQ3UQ84. GQKVDAV.

Enzyme and pathway databases

BRENDA6.1.1.3. 244.

Gene expression databases

ArrayExpressQ3UQ84.
BgeeQ3UQ84.
GermOnlineENSMUSG00000028107. Mus musculus.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR012675. b-grasp_ferredoxin-like.
IPR004095. TGS.
IPR002320. Thr-tRNA-synth_IIa.
IPR018158. Thr-tRNA-synth_IIa_cons-reg.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio334572.
SOURCESearch...

Entry information

Entry nameSYTM_MOUSE
AccessionPrimary (citable) accession number: Q3UQ84
Secondary accession number(s): Q9D0D6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 11, 2005
Last modified: June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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