Serine--tRNA ligase, mitochondrial precursor

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Q9N0F3 (SYSM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	seryl-tRNA aminoacylation Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB serine-tRNA ligase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 34

Mitochondrion Ref.1

Chain

35 – 518

484

Serine--tRNA ligase, mitochondrial

PRO_0000035821

Regions

Nucleotide binding

330 – 332

ATP

Nucleotide binding

418 – 421

ATP

Region

299 – 301

Serine binding

Sites

Binding site

345

ATP; via amide nitrogen and carbonyl oxygen

Binding site

352

Serine

Binding site

453

Serine

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

110

N6-acetyllysine By similarity

Experimental info

Sequence conflict

438

Q → H in AAX46747. Ref.2

Secondary structure

518

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9N0F3 [UniParc].

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

FASTA

518

58,296

        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

References

	« Hide 'large scale' referencesShow '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.

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.

IPI

IPI00698619.

RefSeq

NP_776882.1. NM_174457.2.

UniGene

Bt.8850.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WLE	X-ray	1.65	A/B	35-518	[»]

ProteinModelPortal

Q9N0F3.

SMR

Q9N0F3. Positions 39-507.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9N0F3.

Proteomic databases

PRIDE

Q9N0F3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

282060.

KEGG

bta:282060.

Organism-specific databases

CTD

54938.

Phylogenomic databases

eggNOG

maNOG13231.

GeneTree

ENSGT00550000075125.

HOVERGEN

HBG023869.

InParanoid

Q9N0F3.

OrthoDB

EOG4KD6KZ.

PhylomeDB

Q9N0F3.

Enzyme and pathway databases

BRENDA

6.1.1.11. 908.

Family and domain databases

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-synth_IIa.
IPR010978. tRNA-bd_arm.
[Graphical view]

K01875.

PANTHER

PTHR11778. tRNA-synt_ser. 1 hit.

Pfam

PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]

PIRSF

PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.

PRINTS

PR00981. TRNASYNTHSER.

SUPFAM

SSF46589. tRNA_binding_arm. 1 hit.

TIGRFAMs

TIGR00414. SerS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYSM_BOVIN

Accession

Primary (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:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents