ID   A0A0K0DNH4_ANGCA        Unreviewed;       373 AA.
AC   A0A0K0DNH4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0001331101-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0001331101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594}.
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DR   AlphaFoldDB; A0A0K0DNH4; -.
DR   STRING; 6313.A0A0K0DNH4; -.
DR   WBParaSite; ACAC_0001331101-mRNA-1; ACAC_0001331101-mRNA-1; ACAC_0001331101.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
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   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43740:SF3; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00133; tRNA-synt_1; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035642}.
FT   DOMAIN          208..244
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
SQ   SEQUENCE   373 AA;  41853 MW;  DD7E24822312FD53 CRC64;
     MPVIVVPDNY DGPAMNLDAR QRAWGTPIPM ILSADGKTAV PLSDGELPLI QGRNAGEKVT
     CDRLEGGEGY FEKDTLDTFF DSSWYYLRYL DPKNEHAPLS VEAATKMPVD IYVGGIEHGS
     SFLRLYSSFK YFISAAVHMF FARFMSYFLA DIGVVQELEP FRNIIPQGIV RGKTYVDKQG
     RYFPKSEIIM KENKCFSADG VELEAVFEKM SKSKRNGIDP LDVLSKNGVD ITRLQLIDSA
     APRQPVNWEE SGLCTDRLSI CYLIISVSMC LEVLKLHNTA LARLQGFTNS LRKLDASVLG
     LSLEAERSIY ALVTMMQVFV PYTASELWAA LQLVHPIKKA VSRPFFVDEM SWPQVDPDCS
     IDFMILVSLT FGF
//