ID SYKM_YEAST Reviewed; 576 AA.
AC P32048; D6W1A6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 27-MAR-2024, entry version 192.
DE RecName: Full=Lysine--tRNA ligase, mitochondrial;
DE EC=6.1.1.6 {ECO:0000305|PubMed:2016746};
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
DE Flags: Precursor;
GN Name=MSK1; OrderedLocusNames=YNL073W; ORFNames=N2364;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2016746; DOI=10.1016/0022-2836(91)90701-7;
RA Gatti D., Tzagoloff A.;
RT "Structure and evolution of a group of related aminoacyl-tRNA
RT synthetases.";
RL J. Mol. Biol. 218:557-568(1991).
RN [2]
RP SEQUENCE REVISION.
RA Tzagoloff A.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701611;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA Poehlmann R., Philippsen P.;
RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT ORFs.";
RL Yeast 12:391-402(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the attachment of lysine to tRNA(Lys) in the
CC mitochondrion. {ECO:0000269|PubMed:2016746}.
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 Evidence={ECO:0000305|PubMed:2016746};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20793;
CC Evidence={ECO:0000305|PubMed:2016746};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:2016746}.
CC -!- MISCELLANEOUS: Present with 2280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; X57360; CAA40634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X86470; CAA60187.1; -; Genomic_DNA.
DR EMBL; Z71349; CAA95947.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10472.1; -; Genomic_DNA.
DR PIR; S14834; S14834.
DR RefSeq; NP_014326.1; NM_001182911.1.
DR AlphaFoldDB; P32048; -.
DR SMR; P32048; -.
DR BioGRID; 35750; 136.
DR DIP; DIP-5319N; -.
DR IntAct; P32048; 2.
DR MINT; P32048; -.
DR STRING; 4932.YNL073W; -.
DR iPTMnet; P32048; -.
DR MaxQB; P32048; -.
DR PaxDb; 4932-YNL073W; -.
DR PeptideAtlas; P32048; -.
DR EnsemblFungi; YNL073W_mRNA; YNL073W; YNL073W.
DR GeneID; 855651; -.
DR KEGG; sce:YNL073W; -.
DR AGR; SGD:S000005017; -.
DR SGD; S000005017; MSK1.
DR VEuPathDB; FungiDB:YNL073W; -.
DR eggNOG; KOG1885; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_008255_6_0_1; -.
DR InParanoid; P32048; -.
DR OMA; MKWGMPP; -.
DR OrthoDB; 648039at2759; -.
DR BioCyc; YEAST:G3O-33102-MONOMER; -.
DR BRENDA; 6.1.1.6; 984.
DR BioGRID-ORCS; 855651; 7 hits in 10 CRISPR screens.
DR PRO; PR:P32048; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P32048; Protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IMP:SGD.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; ISA:SGD.
DR GO; GO:0070154; P:mitochondrial lysyl-tRNA aminoacylation; IMP:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR GO; GO:0008033; P:tRNA processing; IDA:SGD.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00499; lysS_bact; 1.
DR PANTHER; PTHR42918:SF5; LYSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..576
FT /note="Lysine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035812"
SQ SEQUENCE 576 AA; 66128 MW; E3C440EEF86BB46E CRC64;
MNVLLKRRSL TFAPRWLWCK CRSSRSRPYS LAHAVDTSKM EATRRNGQIV KDLGRYYPSM
SESALHDLCQ EYKEVTIADF NERFLGNPAT LHHEDNPNLL LSINGRIKSI RFSGQKIVFI
DLYNGSSGLK NDTQLQLIVN YNKIGGSSED KANFSEYMNF LKKGDYIKAL GYPGFSQSRV
KMLSLICNKL PIVLSVSQLP LPSRLNDETK IKSNRVVDYQ LNGTQTLLVR ARIIKLLRKF
LDDRNFVEVE TPILSSKSNG AMAKPFITSS KDFDHLELRI APELWLKRLI ISGLQKVYEI
GKVFRNEGID STHNAEFSTL EFYETYMSMD DIVTRTEDLF KFLITNLQKF FQDTRLPVPK
TFSELHLALS ENNWKFRKVE FLPTLNKELG IDLMNSGLDI NKPSELLKAL PKDIAKKYFP
SADNTGQLSS LQILNKLSDV FLEQRHCQST LPTVIYHQPA ILSPLAKTDP QNKQVTKRFE
VFIKGKEYIN AYEEENCPQL QLQKFLQQKQ INELTGNKTE TLSPVIDYQY VETMKYGMPP
VGGFGLGIDR LCMLFCDKKR IEEVLPFGCV DDVNRQ
//
