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Reviewed, UniProtKB/Swiss-Prot Q9N0F3 (SYSM_BOVIN)

Last modified February 9, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
    Seryl-tRNA synthetase, mitochondrial
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
    SerRSmt
Gene names
Name: SARS2
Synonyms: SARSM
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the attachment of serine to tRNA(Ser). Is also probably 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). Ref.1

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). Ref.1

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). Ref.1

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 probably binds across the dimer. Ref.4

Subcellular location

Mitochondrion matrix.

Domain

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

Post-translational modification

Two N-termini starting at positions 35 and 37 have been identified by direct sequencing.

Sequence similarities

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

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processseryl-tRNA aminoacylation Ref.1

Inferred from direct assay. Source: UniProtKB

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding Ref.1

Inferred from direct assay. Source: UniProtKB

serine-tRNA ligase activity Ref.1

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Ref.1
Chain35 – 518484Seryl-tRNA synthetase, mitochondrial
PRO_0000035821

Regions

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

Sites

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

Amino acid modifications

Modified residue521Phosphotyrosine By similarity
Modified residue1101N6-acetyllysine By similarity

Experimental info

Sequence conflict4381Q → H in AAX46747. Ref.2

Secondary structure

1 ............................................................................. 518
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9N0F3-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C4411C953E842595

FASTA51858,296
        10         20         30         40         50         60 
MAASIVRRLG PLVAGRGLRL RGGCVCNQSF KRSFATERQD RNLLYEHARE GYSALPLLDM 

        70         80         90        100        110        120 
ESLCAYPEDA ARALDLRKGE LRSKDLPGII STWQELRQLR EQIRSLEEEK EAVTEAVRAL 

       130        140        150        160        170        180 
VVNQDNSQVQ QDPQYQSLRA RGREIRKQLT LLYPKEAQLE EQFYLRALRL PNQTHPDVPV 

       190        200        210        220        230        240 
GDESQARVLH VVGDKPAFSF QPRGHLEIAE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH 

       250        260        270        280        290        300 
GLVNFTLNKL IHRGFTPMTV PDLLRGVVFE GCGMTPNAKP SQIYNIDPSR FEDLNLAGTA 

       310        320        330        340        350        360 
EVGLAGYFMD HSVAFRDLPI RMVCSSTCYR AETDTGKEPW GLYRVHHFTK VEMFGVTGPG 

       370        380        390        400        410        420 
LEQSSELLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRFGEVT 

       430        440        450        460        470        480 
SASNCTDFQS RRLHIMFQTE AGELQFAHTV NATGCAVPRL LIALLESYQQ KDGSVLVPPA 

       490        500        510 
LQPYLGTDRI TTPTHVPLQY IGPNQPQKPR LPGQPASS

« Hide

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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], PROTEIN SEQUENCE OF 35-55; 111-145; 167-176; 196-211; 396-407 AND 472-500, FUNCTION, CATALYTIC ACTIVITY.
Tissue: Liver.
[2]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.
[4]"Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase in mammalian mitochondria."
Chimnaronk S., Gravers Jeppesen M., Suzuki T., Nyborg J., Watanabe K.
EMBO J. 24:3369-3379(2005) [PubMed: 16163389] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 35-518 IN COMPLEX WITH SUBSTRATE, SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB029947 mRNA. Translation: BAA99556.1.
BT021565 mRNA. Translation: AAX46412.1.
BT021900 mRNA. Translation: AAX46747.1.
BC140548 mRNA. Translation: AAI40549.1.
IPIIPI00698619.
RefSeqNP_776882.1.
UniGeneBt.8850

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLEX-ray1.65A/B35-518[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9N0F3.

Genome annotation databases

EnsemblENSBTAT00000002334; ENSBTAP00000002334; ENSBTAG00000001780; Bos taurus. [Genome view]
GeneID282060.
KEGGbta:282060.

Organism-specific databases

CTD282060.

Phylogenomic databases

eggNOGmaNOG13231.
HOVERGENQ9N0F3.
InParanoidQ9N0F3.
PhylomeDBQ9N0F3.

Enzyme and pathway databases

BRENDA6.1.1.11. 251.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR002317. Ser-tRNA-synth_IIa.
IPR018156. Ser-tRNA-synth_IIa_C.
IPR010978. tRNA_bd_arm.
[Graphical view]
PANTHERPTHR11778. tRNA-synt_ser. 1 hit.
PfamPF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYSM_BOVIN
AccessionPrimary (citable) accession number: Q9N0F3
Secondary accession number(s): A5D7G7, Q58CP7, Q58DN2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 64 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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