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Protein

Serine--tRNA ligase, mitochondrial

Gene

Sars2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Pathwayi: selenocysteinyl-tRNA(Sec) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-seryl-tRNA(Sec) from L-serine and tRNA(Sec).
Proteins known to be involved in this subpathway in this organism are:
  1. Serine--tRNA ligase, cytoplasmic (Sars), Serine--tRNA ligase, mitochondrial (Sars2)
This subpathway is part of the pathway selenocysteinyl-tRNA(Sec) biosynthesis, which is itself part of Aminoacyl-tRNA biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-seryl-tRNA(Sec) from L-serine and tRNA(Sec), the pathway selenocysteinyl-tRNA(Sec) biosynthesis and in Aminoacyl-tRNA biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei345 – 3451ATP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei352 – 3521SerineBy similarity
Binding sitei453 – 4531SerineBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi330 – 3323ATPBy similarity
Nucleotide bindingi418 – 4214ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI
  • serine-tRNA ligase activity Source: UniProtKB

GO - Biological processi

  • selenocysteinyl-tRNA(Sec) biosynthetic process Source: UniProtKB-UniPathway
  • seryl-tRNA aminoacylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.11. 3474.
UniPathwayiUPA00906; UER00895.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Sars2
Synonyms:Sarsm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1919234. Sars2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionBy similarityAdd
BLAST
Chaini35 – 518484Serine--tRNA ligase, mitochondrialPRO_0000035823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-acetyllysineCombined sources
Modified residuei195 – 1951N6-succinyllysineCombined sources
Modified residuei337 – 3371N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9JJL8.
MaxQBiQ9JJL8.
PaxDbiQ9JJL8.
PeptideAtlasiQ9JJL8.
PRIDEiQ9JJL8.

PTM databases

iPTMnetiQ9JJL8.
PhosphoSiteiQ9JJL8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000070699.
CleanExiMM_SARS2.
GenevisibleiQ9JJL8. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9JJL8. 1 interaction.
MINTiMINT-4136515.
STRINGi10090.ENSMUSP00000092216.

Structurei

3D structure databases

ProteinModelPortaliQ9JJL8.
SMRiQ9JJL8. Positions 41-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni299 – 3013Serine bindingBy similarity

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2509. Eukaryota.
COG0172. LUCA.
GeneTreeiENSGT00790000123121.
HOGENOMiHOG000035937.
HOVERGENiHBG023869.
InParanoidiQ9JJL8.
KOiK01875.
OMAiYPKETQL.
OrthoDBiEOG091G05BT.
TreeFamiTF315020.

Family and domain databases

CDDicd00770. SerRS_core. 1 hit.
Gene3Di1.10.287.40. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR033729. SerRS_core.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERiPTHR11778. PTHR11778. 1 hit.
PfamiPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSiPR00981. TRNASYNTHSER.
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00414. serS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JJL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASMARLWW PFLARQGLRS RGRCVCSQNP RRSFATEKRV RNLLYEHARE
60 70 80 90 100
GYSELPYLDM ESVCACPEKA ARSLELRKGE LRPADLPAII STWQELRQLR
110 120 130 140 150
EQIRSLEAEK EAVAEAVRAL LANQDSDQVQ KDPQYQGLRA RGREIRKQLT
160 170 180 190 200
PLYPQETQLE EQLYQQALRL PNQTHPDTPV GDESQARVVR VVGEKPAFSF
210 220 230 240 250
QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH GLVNFTLSKL
260 270 280 290 300
VSRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPSR FEDLNLAGTA
310 320 330 340 350
EVGLAGYFMD HSVAFRDLPV RMVCASTCYR AETDTGKEPW GLYRVHHFTK
360 370 380 390 400
VEMFGVTGPG LEQSSQLLDE FLSLQVEILT ELGLHFRVLD MPTQELGLPA
410 420 430 440 450
YRKFDIEAWM PGRGRYGEVT SASNCTDFQS RRLYIMFETE TGELQFAHTV
460 470 480 490 500
NATACAVPRV LIALLESNQQ KDGSVLVPAA LQPYLGTDRI TAPTHVPLQY
510
IGPNQPQKPR LPGQSATR
Length:518
Mass (Da):58,316
Last modified:July 27, 2011 - v2
Checksum:iB3D988AD96B49E90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2371L → V in BAA99558 (PubMed:10764807).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21053.1.
RefSeqiNP_076126.2. NM_023637.3.
UniGeneiMm.333725.

Genome annotation databases

EnsembliENSMUST00000094632; ENSMUSP00000092216; ENSMUSG00000070699.
GeneIDi71984.
KEGGimmu:71984.
UCSCiuc009fzq.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21053.1.
RefSeqiNP_076126.2. NM_023637.3.
UniGeneiMm.333725.

3D structure databases

ProteinModelPortaliQ9JJL8.
SMRiQ9JJL8. Positions 41-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JJL8. 1 interaction.
MINTiMINT-4136515.
STRINGi10090.ENSMUSP00000092216.

PTM databases

iPTMnetiQ9JJL8.
PhosphoSiteiQ9JJL8.

Proteomic databases

EPDiQ9JJL8.
MaxQBiQ9JJL8.
PaxDbiQ9JJL8.
PeptideAtlasiQ9JJL8.
PRIDEiQ9JJL8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094632; ENSMUSP00000092216; ENSMUSG00000070699.
GeneIDi71984.
KEGGimmu:71984.
UCSCiuc009fzq.3. mouse.

Organism-specific databases

CTDi54938.
MGIiMGI:1919234. Sars2.

Phylogenomic databases

eggNOGiKOG2509. Eukaryota.
COG0172. LUCA.
GeneTreeiENSGT00790000123121.
HOGENOMiHOG000035937.
HOVERGENiHBG023869.
InParanoidiQ9JJL8.
KOiK01875.
OMAiYPKETQL.
OrthoDBiEOG091G05BT.
TreeFamiTF315020.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895.
BRENDAi6.1.1.11. 3474.

Miscellaneous databases

PROiQ9JJL8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000070699.
CleanExiMM_SARS2.
GenevisibleiQ9JJL8. MM.

Family and domain databases

CDDicd00770. SerRS_core. 1 hit.
Gene3Di1.10.287.40. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR033729. SerRS_core.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERiPTHR11778. PTHR11778. 1 hit.
PfamiPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSiPR00981. TRNASYNTHSER.
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00414. serS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYSM_MOUSE
AccessioniPrimary (citable) accession number: Q9JJL8
Secondary accession number(s): Q68FL2, Q9CWP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.