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Protein

Serine--tRNA ligase, mitochondrial

Gene

SARS2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

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, mitochondrial (SARS2), Serine--tRNA ligase, cytoplasmic (SARS)
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)DescriptionActionsGraphical viewLength
Binding sitei345ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei352Serine1
Binding sitei453Serine1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi330 – 332ATP3
Nucleotide bindingi418 – 421ATP4

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • 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. 908.
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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34Mitochondrion1 PublicationAdd BLAST34
ChainiPRO_000003582135 – 518Serine--tRNA ligase, mitochondrialAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei110N6-acetyllysineBy similarity1
Modified residuei195N6-succinyllysineBy similarity1
Modified residuei337N6-succinyllysineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9N0F3.
PRIDEiQ9N0F3.

Expressioni

Gene expression databases

BgeeiENSBTAG00000001780.

Interactioni

Subunit structurei

Homodimer. The tRNA molecule probably binds across the dimer.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002334.

Structurei

Secondary structure

1518
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 49Combined sources7
Helixi60 – 65Combined sources6
Helixi67 – 77Combined sources11
Helixi83 – 85Combined sources3
Helixi86 – 124Combined sources39
Helixi129 – 131Combined sources3
Helixi133 – 167Combined sources35
Helixi183 – 185Combined sources3
Beta strandi187 – 193Combined sources7
Helixi205 – 211Combined sources7
Turni221 – 224Combined sources4
Beta strandi230 – 232Combined sources3
Helixi234 – 252Combined sources19
Beta strandi256 – 259Combined sources4
Beta strandi262 – 264Combined sources3
Helixi266 – 272Combined sources7
Beta strandi276 – 280Combined sources5
Turni288 – 290Combined sources3
Beta strandi291 – 293Combined sources3
Helixi300 – 308Combined sources9
Beta strandi311 – 314Combined sources4
Helixi315 – 317Combined sources3
Beta strandi319 – 329Combined sources11
Beta strandi341 – 344Combined sources4
Beta strandi346 – 357Combined sources12
Helixi361 – 381Combined sources21
Beta strandi386 – 390Combined sources5
Helixi393 – 395Combined sources3
Turni397 – 399Combined sources3
Beta strandi401 – 410Combined sources10
Turni411 – 414Combined sources4
Beta strandi415 – 424Combined sources10
Helixi428 – 433Combined sources6
Beta strandi436 – 438Combined sources3
Beta strandi440 – 442Combined sources3
Beta strandi444 – 446Combined sources3
Beta strandi448 – 456Combined sources9
Helixi457 – 468Combined sources12
Helixi479 – 481Combined sources3
Helixi482 – 485Combined sources4
Beta strandi486 – 490Combined sources5
Beta strandi502 – 505Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLEX-ray1.65A/B35-518[»]
ProteinModelPortaliQ9N0F3.
SMRiQ9N0F3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9N0F3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni299 – 301Serine binding3

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.
HOGENOMiHOG000035937.
HOVERGENiHBG023869.
InParanoidiQ9N0F3.
KOiK01875.

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.
PfamiPF00587. 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.

Q9N0F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASIVRRLG PLVAGRGLRL RGGCVCNQSF KRSFATERQD RNLLYEHARE
60 70 80 90 100
GYSALPLLDM ESLCAYPEDA ARALDLRKGE LRSKDLPGII STWQELRQLR
110 120 130 140 150
EQIRSLEEEK EAVTEAVRAL VVNQDNSQVQ QDPQYQSLRA RGREIRKQLT
160 170 180 190 200
LLYPKEAQLE EQFYLRALRL PNQTHPDVPV GDESQARVLH VVGDKPAFSF
210 220 230 240 250
QPRGHLEIAE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH GLVNFTLNKL
260 270 280 290 300
IHRGFTPMTV PDLLRGVVFE GCGMTPNAKP SQIYNIDPSR FEDLNLAGTA
310 320 330 340 350
EVGLAGYFMD HSVAFRDLPI RMVCSSTCYR AETDTGKEPW GLYRVHHFTK
360 370 380 390 400
VEMFGVTGPG LEQSSELLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA
410 420 430 440 450
YRKFDIEAWM PGRGRFGEVT SASNCTDFQS RRLHIMFQTE AGELQFAHTV
460 470 480 490 500
NATGCAVPRL LIALLESYQQ KDGSVLVPPA LQPYLGTDRI TTPTHVPLQY
510
IGPNQPQKPR LPGQPASS
Length:518
Mass (Da):58,296
Last modified:October 1, 2000 - v1
Checksum:iC4411C953E842595
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti438Q → H in AAX46747 (PubMed:16305752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029947 mRNA. Translation: BAA99556.1.
BT021565 mRNA. Translation: AAX46412.1.
BT021900 mRNA. Translation: AAX46747.1.
BC140548 mRNA. Translation: AAI40549.1.
RefSeqiNP_776882.1. NM_174457.3.
UniGeneiBt.8850.

Genome annotation databases

GeneIDi282060.
KEGGibta:282060.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029947 mRNA. Translation: BAA99556.1.
BT021565 mRNA. Translation: AAX46412.1.
BT021900 mRNA. Translation: AAX46747.1.
BC140548 mRNA. Translation: AAI40549.1.
RefSeqiNP_776882.1. NM_174457.3.
UniGeneiBt.8850.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLEX-ray1.65A/B35-518[»]
ProteinModelPortaliQ9N0F3.
SMRiQ9N0F3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002334.

Proteomic databases

PaxDbiQ9N0F3.
PRIDEiQ9N0F3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282060.
KEGGibta:282060.

Organism-specific databases

CTDi54938.

Phylogenomic databases

eggNOGiKOG2509. Eukaryota.
COG0172. LUCA.
HOGENOMiHOG000035937.
HOVERGENiHBG023869.
InParanoidiQ9N0F3.
KOiK01875.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895.
BRENDAi6.1.1.11. 908.

Miscellaneous databases

EvolutionaryTraceiQ9N0F3.

Gene expression databases

BgeeiENSBTAG00000001780.

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.
PfamiPF00587. 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_BOVIN
AccessioniPrimary (citable) accession number: Q9N0F3
Secondary accession number(s): A5D7G7, Q58CP7, Q58DN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.