SYK_CAEEL
ID SYK_CAEEL Reviewed; 572 AA.
AC Q22099;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=kars-1 {ECO:0000312|WormBase:T02G5.9a};
GN Synonyms=krs-1 {ECO:0000312|WormBase:T02G5.9a};
GN ORFNames=T02G5.9 {ECO:0000312|WormBase:T02G5.9a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=23692540; DOI=10.1111/acel.12101;
RA Rousakis A., Vlassis A., Vlanti A., Patera S., Thireos G., Syntichaki P.;
RT "The general control nonderepressible-2 kinase mediates stress response and
RT longevity induced by target of rapamycin inactivation in Caenorhabditis
RT elegans.";
RL Aging Cell 12:742-751(2013).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. {ECO:0000250|UniProtKB:Q15046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an arrest at
CC an early larval stage. In adults, causes a 80 percent reduction in
CC progeny size and a 50 percent increase in eIF2alpha phosphorylation.
CC {ECO:0000269|PubMed:23692540}.
CC -!- MISCELLANEOUS: It is likely that the same gene provides both this
CC cytoplasmic isoform and an additional mitochondrial isoform.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; FO081112; CCD69180.1; -; Genomic_DNA.
DR PIR; T16780; T16780.
DR RefSeq; NP_495453.1; NM_063052.4.
DR AlphaFoldDB; Q22099; -.
DR SMR; Q22099; -.
DR BioGRID; 39496; 5.
DR STRING; 6239.T02G5.9b; -.
DR EPD; Q22099; -.
DR PaxDb; Q22099; -.
DR PeptideAtlas; Q22099; -.
DR EnsemblMetazoa; T02G5.9a.1; T02G5.9a.1; WBGene00002238.
DR GeneID; 174159; -.
DR KEGG; cel:CELE_T02G5.9; -.
DR UCSC; T02G5.9c.1; c. elegans.
DR CTD; 174159; -.
DR WormBase; T02G5.9a; CE04861; WBGene00002238; kars-1.
DR eggNOG; KOG1885; Eukaryota.
DR InParanoid; Q22099; -.
DR PRO; PR:Q22099; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002238; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q22099; baseline and differential.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0061063; P:positive regulation of nematode larval development; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
DR CDD; cd00775; LysRS_core; 1.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR034762; Lys-tRNA-ligase_II_bac/euk.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PIRSF; PIRSF039101; LysRS2; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00499; lysS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..572
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152767"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 310..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 474..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 530..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 572 AA; 65136 MW; 358511F76A5B1EEF CRC64;
MSEPEAKLSK NEQKRLAKQA KKEQERLEKD AAKLNVAVAD APKVVREADP SDPQEYFNMR
VRMIEARRAA GDNPFPHKFN VTISLTDFIT KYTPLEKEQV VEEIVSVAGR IHSKRESGSK
LVFYDIHGEG THIQIMANAK FHTGDVDFVT LHDRIKRGDI VGFTGRATRT KAGELSLIPN
EILQLTPCLH MLPHSHFGLK DKELRFRKRY LDLILNPRVK DNFVIRSKII TFLRRYLDNL
GFLEVETPIM NQIAGGATAK PFITHHNDLD MNLFLRVAPE LYHKMLVVGG IDRVYEVGRL
FRNEGIDLTH NPEFTTCEFY MAYADYEDVI QLTEDLLSSM VMSIKGTYKI EYHPNGPNTE
PVYEVDFTPP FKRVHMYDGL AEKLGATLPD PSTLHTEEAR EVFDKLCRDN NVDCSAPRTT
ARLLDKLVGE YLESTFISPT FLIGHPQIMS PLAKWHRSIP GLTERFELFA VTREIANAYT
ELNDPITQRQ RFEQQAKDKD AGDDEAQMID ETFCNALEYG LPPTGGWGMG IDRLSMILTD
NNNIKEVLLF PAMRPEDGTE KKTDFDAPTT LA
