SYLM_YEAST
ID SYLM_YEAST Reviewed; 894 AA.
AC P11325; D6VZ17;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Leucine--tRNA ligase, mitochondrial;
DE EC=6.1.1.4 {ECO:0000269|PubMed:1990003};
DE AltName: Full=Leucyl-tRNA synthetase;
DE Short=LeuRS;
DE Flags: Precursor;
GN Name=NAM2; Synonyms=MSL1; OrderedLocusNames=YLR382C; ORFNames=L3502.6;
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].
RX PubMed=2826465; DOI=10.1016/s0021-9258(19)35432-8;
RA Tzagoloff A., Akai A., Kurkulos M., Repetto B.;
RT "Homology of yeast mitochondrial leucyl-tRNA synthetase and isoleucyl- and
RT methionyl-tRNA synthetases of Escherichia coli.";
RL J. Biol. Chem. 263:850-856(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AB1-4A/8/55;
RX PubMed=3034607; DOI=10.1002/j.1460-2075.1987.tb04812.x;
RA Labouesse M., Herbert C.J., Dujardin G., Slonimski P.P.;
RT "Three suppressor mutations which cure a mitochondrial RNA maturase
RT deficiency occur at the same codon in the open reading frame of the nuclear
RT NAM2 gene.";
RL EMBO J. 6:713-721(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 10-31, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=1990003; DOI=10.1016/s0021-9258(18)52278-x;
RA Zagorski W., Castaing B., Herbert C.J., Labouesse M., Martin R.,
RA Slonimski P.P.;
RT "Purification and characterization of the Saccharomyces cerevisiae
RT mitochondrial leucyl-tRNA synthetase.";
RL J. Biol. Chem. 266:2537-2541(1991).
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 leucine to tRNA(Leu) in the
CC mitochondrion. {ECO:0000269|PubMed:1990003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000269|PubMed:1990003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11689;
CC Evidence={ECO:0000269|PubMed:1990003};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for leucine {ECO:0000269|PubMed:1990003};
CC KM=1.02 uM for tRNA {ECO:0000269|PubMed:1990003};
CC pH dependence:
CC Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:1990003};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:1990003};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:1990003}.
CC -!- MISCELLANEOUS: PubMed:3034607 authors identified this protein as the
CC gene product of the NAM2 gene, which is capable of compensating for
CC mutations in mRNA maturase encoded by the fourth intron of the
CC mitochondrial cytochrome b gene. {ECO:0000305|PubMed:3034607}.
CC -!- MISCELLANEOUS: Present with 2120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; J03495; AAA34805.1; -; Genomic_DNA.
DR EMBL; X05143; CAA28791.1; -; Genomic_DNA.
DR EMBL; U19104; AAB67277.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09683.1; -; Genomic_DNA.
DR PIR; A28521; SYBYLM.
DR RefSeq; NP_013486.3; NM_001182271.3.
DR AlphaFoldDB; P11325; -.
DR SMR; P11325; -.
DR BioGRID; 31641; 75.
DR ComplexPortal; CPX-1314; bI4 intron splicing factor complex.
DR IntAct; P11325; 2.
DR MINT; P11325; -.
DR STRING; 4932.YLR382C; -.
DR MoonProt; P11325; -.
DR CarbonylDB; P11325; -.
DR MaxQB; P11325; -.
DR PaxDb; P11325; -.
DR PRIDE; P11325; -.
DR EnsemblFungi; YLR382C_mRNA; YLR382C; YLR382C.
DR GeneID; 851098; -.
DR KEGG; sce:YLR382C; -.
DR SGD; S000004374; NAM2.
DR VEuPathDB; FungiDB:YLR382C; -.
DR eggNOG; KOG0435; Eukaryota.
DR GeneTree; ENSGT00390000015114; -.
DR HOGENOM; CLU_004427_2_0_1; -.
DR InParanoid; P11325; -.
DR OMA; DIDWADV; -.
DR BioCyc; YEAST:G3O-32448-MON; -.
DR PRO; PR:P11325; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P11325; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IDA:SGD.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IPI:SGD.
DR GO; GO:0000372; P:Group I intron splicing; IDA:ComplexPortal.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IGI:SGD.
DR GO; GO:0006397; P:mRNA processing; IDA:ComplexPortal.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Direct protein sequencing; Ligase;
KW Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..9
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1990003"
FT CHAIN 10..894
FT /note="Leucine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035810"
FT MOTIF 56..66
FT /note="'HIGH' region"
FT MOTIF 646..650
FT /note="'KMSKS' region"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 894 AA; 101920 MW; 3862CEFFFB10B262 CRC64;
MLSRPSSRFL STKRGPGPAV KKLIAIGEKW KQKTTRGLPK QDTLNSGSKY ILCQFPYPSG
ALHIGHLRVY VISDSLNRFY KQKGYNVIHP MGWDAFGLPA ENAAIERSIN PAIWTRDNIA
KMKQQMQSML ANFDWDREIT TCDPEYYKFT QWIFLKLFEN GLAYRKEAEI NWDPVDMTVL
ANEQVDAQGR SWRSGAIVEK KQLKQWFLGI TKFAPKLKKH LNQLKDWPSN VKQMQKNWIG
ESVGAELVFK VADPKFENLI VFTTRPETLF AVQYVALALD HPIVQKYCEE MPDLKEFIQK
SDQLPNDTKE GFQLPNIKAV NPLTKEEVPI FAAPYVVSSY GSAPSAVMGC PGHDNRDFEF
WQTNCPGEHI KTCIAPFFDD ASKVTEQERQ RIIDTVPFTS TDGVLTKECG EHSGVLTVVA
RKSIMGMLNS EGLSKSVVRY KIRDWLISRQ RYWGTPIPII HCDNCGPVPV PESDLPVKLP
ELEGLDTKGN PLSTIDEFVN VACPSCGSPA KRETDTMDTF IDSSWYYFRF LDPKNTSKPF
DREIASKNMP VDIYIGGVEH AILHLLYSRF IAKFLGSINA WSDPAGIFEP FKKLVTQGMV
QGKTYVDPDS GKFLKPDELT FVNDSPDGNT VIIKSNGKVP VVSYEKMSKS KYNGADPNEC
ILRHGPDATR AHILFQSPIA DALNWDESKI VGIERWLQKV LHLTKNILSL EKDLAISKDY
KTPTDLNDAE VKFHNDFQRF LKSITESFEV NLSLNTVISD YMKLTNILES ALKKGEVRNE
MIVQNLQKLV TVIYPAVPSI SEEAAEMINS QMEWNQYRWP EVERTTESKF KKFQIVVNGR
VKFMYTADKN FLKLGRDAVI ETLMNLPEGR MYLMNKKIKK FVMKFNVISF LFHK
