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Q3U186 (SYRM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable arginine--tRNA ligase, mitochondrial

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:Rars2
Synonyms:Rarsl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1616Mitochondrion Potential
Chain17 – 578562Probable arginine--tRNA ligase, mitochondrial
PRO_0000250732

Regions

Motif133 – 14412"HIGH" region

Amino acid modifications

Modified residue5681N6-acetyllysine Ref.3

Experimental info

Sequence conflict3061D → G in AAH24878. Ref.2
Sequence conflict5401Q → K in AAH24878. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3U186 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 5255FAFA8F873C27

FASTA57865,336
        10         20         30         40         50         60 
MACGFRRSIA CQLSRVLALP PESLIKSISA VPVSKKEEVA DFQLSVDSLL EDNNHKSQVD 

        70         80         90        100        110        120 
TQDQARRLAE KLKCDTVVTA ISAGPRTLNF KINRELLTKA VLQQVTEDGC KYGLKSELFS 

       130        140        150        160        170        180 
DLPKKRIVVE FSSPNIAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY IGDWGMQFGL 

       190        200        210        220        230        240 
LGTGFQLFGY EEKLQTNPLQ HLFDVYVQVN KEATDDKNVT KLAHEFFHRL EMGDTQALSL 

       250        260        270        280        290        300 
WQRFRDLSIE EYTQIYKRLG IYFDEYSGES FYREKSQDVL KLLDSKGLLQ KTAEGNVVVD 

       310        320        330        340        350        360 
LSGTGDLSSV CTVMRSDGTS LYATRDLAAA IHRMDKYNFD TMIYVADKGQ RRHFQQVFQM 

       370        380        390        400        410        420 
LKIMGYDWAE RCQHVPFGIV KGMKTRRGGV TFLEDVLNEV QSRMLQNMAS IKTTKQLENP 

       430        440        450        460        470        480 
QETAERVGLA AVIIQDFRGT LLSDYQFSWD RVFQSRGDTG VFLQYTHARL CSLEETFGCG 

       490        500        510        520        530        540 
YLNDSNVACL QEPQSVSILQ HLLRFDEVLY LSSQDLQPKH IVSYLLTLSH LAAVAHKTLQ 

       550        560        570 
VKDSPPDVAG ARLHLFKAVR SVLANGMKLL GITPVCRM 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
[3]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-568, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK156182 mRNA. Translation: BAE33614.1.
BC024878 mRNA. Translation: AAH24878.1.
RefSeqNP_852071.2. NM_181406.3.
UniGeneMm.22363.

3D structure databases

ProteinModelPortalQ3U186.
SMRQ3U186. Positions 3-578.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3U186.

Proteomic databases

PaxDbQ3U186.
PRIDEQ3U186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029968; ENSMUSP00000029968; ENSMUSG00000028292.
GeneID109093.
KEGGmmu:109093.
UCSCuc008sgf.2. mouse.

Organism-specific databases

CTD57038.
MGIMGI:1923596. Rars2.

Phylogenomic databases

eggNOGCOG0018.
GeneTreeENSGT00530000063407.
HOGENOMHOG000247211.
HOVERGENHBG057355.
InParanoidQ3U186.
KOK01887.
OMAARLHLFK.
OrthoDBEOG7DNNTT.
PhylomeDBQ3U186.
TreeFamTF300888.

Gene expression databases

ArrayExpressQ3U186.
BgeeQ3U186.
GenevestigatorQ3U186.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio361640.
PROQ3U186.
SOURCESearch...

Entry information

Entry nameSYRM_MOUSE
AccessionPrimary (citable) accession number: Q3U186
Secondary accession number(s): Q8QZU7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries