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Database: UniProt
Entry: A0A2C9KTQ0_BIOGL
LinkDB: A0A2C9KTQ0_BIOGL
Original site: A0A2C9KTQ0_BIOGL 
ID   A0A2C9KTQ0_BIOGL        Unreviewed;       256 AA.
AC   A0A2C9KTQ0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN   Name=106066636 {ECO:0000313|EnsemblMetazoa:BGLB023436-PA};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB023436-PA, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB023436-PA}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB023436-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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}.
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DR   RefSeq; XP_013081159.1; XM_013225705.1.
DR   AlphaFoldDB; A0A2C9KTQ0; -.
DR   STRING; 6526.A0A2C9KTQ0; -.
DR   EnsemblMetazoa; BGLB023436-RA; BGLB023436-PA; BGLB023436.
DR   KEGG; bgt:106066636; -.
DR   VEuPathDB; VectorBase:BGLB023436; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000076420; 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   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
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}.
FT   DOMAIN          38..97
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          147..247
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   256 AA;  29153 MW;  72DF77A07C83E337 CRC64;
     MLSSKEPFKN LLTQGMVKSE SYRVSKTGKY IPKDQVDFSG QSPVEKSTGE ALVVEFEKMS
     KSKYNGVNPE DVLSEYGVDS TRLCILSNVS PQSERNWSEI VYKGVINWQN KIWTLVTNIR
     KYHETNSSSW QEGNITEKDL TDWEKQIDET RNHIINKVTH EFDNTFHINA AISRLHTYVS
     WLGKVPAGAQ GTKAYERALG DLIVMIGVMA PHFASELWTG LADVATFQTH DWKSSVLNQP
     WPKLDQDFLM PLTYSV
//
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