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Reviewed, UniProtKB/Swiss-Prot Q499X9 (SYMM_MOUSE)

Last modified June 16, 2009. Version 40. 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

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Names and origin

Protein namesRecommended name:
    Methionyl-tRNA synthetase, mitochondrial
    EC=6.1.1.10
Alternative name(s):
    Mitochondrial methionine--tRNA ligase
      Short name=MtMetRS
    Methionine--tRNA ligase 2
Gene names
Name: Mars2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological processmethionyl-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

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 586540Methionyl-tRNA synthetase, mitochondrial
PRO_0000045494

Regions

Motif45 – 5511"HIGH" region
Motif340 – 3445"KMSKS" region

Sites

Binding site3431ATP By similarity

Experimental info

Sequence conflict3061L → F in AAH99669. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q499X9-1 [UniParc].

Last modified January 10, 2006. Version 2.
Checksum: 639695ECEE842EFB

FASTA58665,805
        10         20         30         40         50         60 
MLRQCARWVL TRTRFGRGCR RYGSCSPSAS GDAGEARAYF TTPIFYVNAA PHIGHLYSAL 

        70         80         90        100        110        120 
LADALCRHRR LRVPGSASTR FSTGTDEHGL KIQQAAATAG LAPIELCDRV SAQFLQLFRE 

       130        140        150        160        170        180 
ADISSTDFIR TTEARHRVAV QHFWGVLEAR GLLYKGIYEG WYCASDECFL PEAKVTRQVG 

       190        200        210        220        230        240 
PSGDPCPVSL ESGHPVSWTK EENYIFKLSQ FREPLQRWLG NNPQAITPEP FHQAVLQWLE 

       250        260        270        280        290        300 
EELPDLSVSR RSSHLHWGIP VPGDDSQTIY VWLDALVNYL TVVGYPDADF KSWWPATSHI 

       310        320        330        340        350        360 
IGKDILKFHA IYWPALLLGA GLRPPHRIYV HSHWTVSGQK MSKSLGNVVD PRTCLDRYTV 

       370        380        390        400        410        420 
DGFRYFLLRQ GVPNWDCDYY DEKVVKLLDS ELADALGGLL NRCTAYRINP SGTYPSFCAA 

       430        440        450        460        470        480 
CFPSEPGLTG PSVRVQAEDY ALVTAVATLP KLVAGYYNDF QIYKALEAVS SCVRQTNGFV 

       490        500        510        520        530        540 
QRHAPWKLNW ESPEDAPWLG TVLHVALECL RVFGTLLQPV TPNLADKLLS RLGVSTTERG 

       550        560        570        580 
LGELYFLPRF YGHPCPFEGR KLGPDTGLLF PRLDQSRTRL VKAHRT

« Hide

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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 and NOD.
Tissue: Cerebellum, Liver and Spleen.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary tumor.

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Cross-references

Sequence databases

AK042888 mRNA. Translation: BAC31393.1. Different initiation.
AK050196 mRNA. Translation: BAC34119.1.
AK172240 mRNA. Translation: BAE42903.1.
BC099669 mRNA. Translation: AAH99669.1.
IPIIPI00226952.
RefSeqNP_780648.1.
UniGeneMm.19223

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000046994. Mus musculus. [Contig view]
GeneID212679.
KEGGmmu:212679.
NMPDRfig|10090.3.peg.356.

Organism-specific databases

MGIMGI:2444136. Mars2.

Phylogenomic databases

HOGENOMQ499X9.
HOVERGENQ499X9.
OMAQ499X9. KMSKYAD.

Enzyme and pathway databases

BRENDA6.1.1.10. 244.

Gene expression databases

ArrayExpressQ499X9.
BgeeQ499X9.
CleanExMM_MARS2.
GermOnlineENSMUSG00000046994. Mus musculus.

Family and domain databases

InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR002304. Met-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR014758. tRNA-synt_met_N.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
TIGRFAMsTIGR00398. metG. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio373664.
SOURCESearch...

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Entry information

Entry nameSYMM_MOUSE
AccessionPrimary (citable) accession number: Q499X9
Secondary accession number(s): Q3T9W7, Q8BWR9, Q8BXY1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: June 16, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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