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Q9JJL8 (SYSM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine--tRNA ligase, mitochondrial
EC=6.1.1.11
Alternative name(s):
SerRSmt
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene names
Name:Sars2
Synonyms:Sarsm
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length518 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 serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity.

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.

Subunit structure

Homodimer. The tRNA molecule binds across the dimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Domain

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

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

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

serine-tRNA ligase activity

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion By similarity
Chain35 – 518484Serine--tRNA ligase, mitochondrial
PRO_0000035823

Regions

Nucleotide binding330 – 3323ATP By similarity
Nucleotide binding418 – 4214ATP By similarity
Region299 – 3013Serine binding By similarity

Sites

Binding site3451ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site3521Serine By similarity
Binding site4531Serine By similarity

Amino acid modifications

Modified residue521Phosphotyrosine By similarity
Modified residue1101N6-acetyllysine By similarity

Experimental info

Sequence conflict2371L → V in BAA99558. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JJL8 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: B3D988AD96B49E90

FASTA51858,316
        10         20         30         40         50         60 
MAASMARLWW PFLARQGLRS RGRCVCSQNP RRSFATEKRV RNLLYEHARE GYSELPYLDM 

        70         80         90        100        110        120 
ESVCACPEKA ARSLELRKGE LRPADLPAII STWQELRQLR EQIRSLEAEK EAVAEAVRAL 

       130        140        150        160        170        180 
LANQDSDQVQ KDPQYQGLRA RGREIRKQLT PLYPQETQLE EQLYQQALRL PNQTHPDTPV 

       190        200        210        220        230        240 
GDESQARVVR VVGEKPAFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH 

       250        260        270        280        290        300 
GLVNFTLSKL VSRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPSR FEDLNLAGTA 

       310        320        330        340        350        360 
EVGLAGYFMD HSVAFRDLPV RMVCASTCYR AETDTGKEPW GLYRVHHFTK VEMFGVTGPG 

       370        380        390        400        410        420 
LEQSSQLLDE FLSLQVEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRYGEVT 

       430        440        450        460        470        480 
SASNCTDFQS RRLYIMFETE TGELQFAHTV NATACAVPRV LIALLESNQQ KDGSVLVPAA 

       490        500        510 
LQPYLGTDRI TAPTHVPLQY IGPNQPQKPR LPGQSATR

« Hide

References

« Hide 'large scale' references
[1]"Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase."
Yokogawa T., Shimada N., Takeuchi N., Benkowski L., Suzuki T., Omori A., Ueda T., Nishikawa K., Spremulli L.L., Watanabe K.
J. Biol. Chem. 275:19913-19920(2000) [PubMed: 10764807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Embryonic stem cell, Head and Oviduct.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB029949 mRNA. Translation: BAA99558.1.
AK010491 mRNA. Translation: BAB26981.1.
AK087606 mRNA. Translation: BAC39943.1.
AK140760 mRNA. Translation: BAE24469.1.
CH466593 Genomic DNA. Translation: EDL24120.1.
BC079664 mRNA. Translation: AAH79664.1.
IPIIPI00109354.
RefSeqNP_076126.2. NM_023637.3.
UniGeneMm.333725.

3D structure databases

ProteinModelPortalQ9JJL8.
SMRQ9JJL8. Positions 41-507.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JJL8.

PTM databases

PhosphoSiteQ9JJL8.

Proteomic databases

PRIDEQ9JJL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000094632; ENSMUSP00000092216; ENSMUSG00000070699.
GeneID71984.
KEGGmmu:71984.

Organism-specific databases

CTD54938.
MGIMGI:1919234. Sars2.

Phylogenomic databases

GeneTreeENSGT00550000075125.
HOGENOMHBG629391.
HOVERGENHBG023869.
InParanoidQ9JJL8.
OrthoDBEOG4KD6KZ.
PhylomeDBQ9JJL8.

Enzyme and pathway databases

BRENDA6.1.1.11. 3474.

Gene expression databases

ArrayExpressQ9JJL8.
BgeeQ9JJL8.
CleanExMM_SARS2.
GenevestigatorQ9JJL8.
GermOnlineENSMUSG00000070699. Mus musculus.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-synth_IIa.
IPR015866. Ser-tRNA-synth_IIa_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
KOK01875.
PANTHERPTHR11778. tRNA-synt_ser. 1 hit.
PfamPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00414. SerS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio335130.
SOURCESearch...

Entry information

Entry nameSYSM_MOUSE
AccessionPrimary (citable) accession number: Q9JJL8
Secondary accession number(s): Q68FL2, Q9CWP1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents