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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei345 – 3451ATP; via amide nitrogen and carbonyl oxygen
Binding sitei352 – 3521Serine
Binding sitei453 – 4531Serine

Regions

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

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434Mitochondrion1 PublicationAdd
BLAST
Chaini35 – 518484Serine--tRNA ligase, mitochondrialPRO_0000035821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-acetyllysineBy similarity
Modified residuei195 – 1951N6-succinyllysineBy similarity
Modified residuei337 – 3371N6-succinyllysineBy similarity

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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002334.

Structurei

Secondary structure

1
518
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 497Combined sources
Helixi60 – 656Combined sources
Helixi67 – 7711Combined sources
Helixi83 – 853Combined sources
Helixi86 – 12439Combined sources
Helixi129 – 1313Combined sources
Helixi133 – 16735Combined sources
Helixi183 – 1853Combined sources
Beta strandi187 – 1937Combined sources
Helixi205 – 2117Combined sources
Turni221 – 2244Combined sources
Beta strandi230 – 2323Combined sources
Helixi234 – 25219Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi262 – 2643Combined sources
Helixi266 – 2727Combined sources
Beta strandi276 – 2805Combined sources
Turni288 – 2903Combined sources
Beta strandi291 – 2933Combined sources
Helixi300 – 3089Combined sources
Beta strandi311 – 3144Combined sources
Helixi315 – 3173Combined sources
Beta strandi319 – 32911Combined sources
Beta strandi341 – 3444Combined sources
Beta strandi346 – 35712Combined sources
Helixi361 – 38121Combined sources
Beta strandi386 – 3905Combined sources
Helixi393 – 3953Combined sources
Turni397 – 3993Combined sources
Beta strandi401 – 41010Combined sources
Turni411 – 4144Combined sources
Beta strandi415 – 42410Combined sources
Helixi428 – 4336Combined sources
Beta strandi436 – 4383Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi444 – 4463Combined sources
Beta strandi448 – 4569Combined sources
Helixi457 – 46812Combined sources
Helixi479 – 4813Combined sources
Helixi482 – 4854Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi502 – 5054Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLEX-ray1.65A/B35-518[»]
ProteinModelPortaliQ9N0F3.
SMRiQ9N0F3. Positions 39-507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9N0F3.

Family & Domainsi

Region

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

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

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti438 – 4381Q → H in AAX46747 (PubMed:16305752).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLEX-ray1.65A/B35-518[»]
ProteinModelPortaliQ9N0F3.
SMRiQ9N0F3. Positions 39-507.
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.
NextBioi20805916.

Family and domain databases

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.
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...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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. 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 35-518 IN COMPLEX WITH SUBSTRATE, SUBUNIT.

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: December 9, 2015
This is version 109 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.