ID A0A0C7MY88_9SACH Unreviewed; 880 AA.
AC A0A0C7MY88;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=LALA0_S01e10704g {ECO:0000313|EMBL:CEP60430.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP60430.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP60430.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP60430.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001372};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; LN736360; CEP60430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7MY88; -.
DR STRING; 1245769.A0A0C7MY88; -.
DR HOGENOM; CLU_004427_0_0_1; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304}.
FT DOMAIN 52..189
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 238..422
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 435..595
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 722..835
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 880 AA; 98947 MW; 009140B7A74B647A CRC64;
MRVSHQCWKW LRRFYGTVPP EEVNLVEIGQ KWKSKVLRGP TVQNVTEKKK KYILSMFPYP
SGSLHIGHLR VYTITDALNR FYKLNGYQVL HPMGWDAFGL PAENAAIERQ IGPASWTQQN
IAKMKQQLNS MLANFDWDRE VTTCSPDYYK FTQKIFLELH KHGLAYQKDA EINWDPVDQT
VLANEQVDSQ GRSWRSGAVV EKRKLKQWFL GITKFAHSLQ KDLQLLDEWP QNVKTMQKNW
IGESYGTEVK FPLSQKDSGQ ITVFTTRVET VFSVQYIALA TKHPLVEKAA LSDPGLKNFL
KHAESLPEDS KEGYLLNSIH AQHPLLSASK KEVPVFVAPY VLSTYGHGAV MGCPAHDQRD
FTFWKHNMPK IEMRPTVVPK NDSPAALREL PYVGKSGVIN CPGSDFDGMD TQVASQAIAT
ALEQKGMGKA TVTYKLRDWL ISRQRFWGAP IPIIHCDDCG SVPVPEQDLP VRLPAVGSLA
GKGSSLKTMH EFVNTTCPSC GSPAKRETDT MDTFMDSSWY FFRYTDPKNT EKPFGFDVAS
KNLPVDLYIG GIEHAILHLL YSRFISKFLA SVGKWGDKLG NGEPFKKLVT QGMVHGRTLI
DPETGRFLKS DEVTSIEGDD LIIKATGQKP SVAYEKMSKS KYNGADPDLC IQTHGADATR
AHILFQAPIS EILSWDEAKI VGVERWLHKV IKLTRKSAIK DSAVNDMKAP TASDHEICFF
NDVQKLLKSI TFSFTESLSL NTVVSDYMKL TNLIENAHHS KLINSTLLTK SLKILITSMY
PITPTVAEEA FSILSGSKSN GWNLYVWPEA EAIKESELVN YQVVINGKMR FTHNAATSFI
NDKDSAIKTL LSSKDGQKYL SGKSIKRVIM RNKVISFVVN
//
