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Database: UniProt
Entry: A0A1A9UK44_GLOAU
LinkDB: A0A1A9UK44_GLOAU
Original site: A0A1A9UK44_GLOAU 
ID   A0A1A9UK44_GLOAU        Unreviewed;       490 AA.
AC   A0A1A9UK44;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
OS   Glossina austeni (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT007412-PA, ECO:0000313|Proteomes:UP000078200};
RN   [1] {ECO:0000313|Proteomes:UP000078200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GAUT007412-PA}
RP   IDENTIFICATION.
RC   STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT007412-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   AlphaFoldDB; A0A1A9UK44; -.
DR   STRING; 7395.A0A1A9UK44; -.
DR   EnsemblMetazoa; GAUT007412-RA; GAUT007412-PA; GAUT007412.
DR   VEuPathDB; VectorBase:GAUT007412; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000078200; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 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}.
FT   DOMAIN          6..44
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          47..208
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          247..282
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          329..451
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   490 AA;  57904 MW;  1FEFCF82719DD6DF CRC64;
     MPDSHYNAIL AVPAYHKDQW NFAKKYNLPI LYVLRDSAGK KTINYKLKDW CISRQRFWGA
     PIPIITNNYG KIFTVSENKL PILLPKQNKN CLFSSLKDYT NWMNVYYDEN RFIRETDTFD
     TFVQSSWYLH RYTCPDYMEG MLNSDSVNYW LPVDLYIGGI EHATMHLLYL RFYHKLFKDM
     NLVNSSEPVK KLLCQGMVLS DTFYYISKEG NQIWTTPKNK DFQRNKNNQI INAVDSLGNK
     LVHIGMNKMS KSKSNGVDPN TIIHQYGADT LRLFIVFAAP PEASLEWTEK GIQGAYRFIK
     KIWNITFNYI KNYRNNKKQN KSKYNNEDLE LMKQTQKIIE KITDNFENKY KFNTVVALIM
     KLTNYLCDAI KNNKCNQLII KQVLMIIIRL LYPFTPHVCF ILWRELNGSQ DIDYAEWPKI
     NYNITETQKK IIVQINGKLK KIMIFNFKSS EKYIKNKILN SSIIKNTLKN KKLKKTIYIK
     NKLINFVLSE
//
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