ID A0A7M4ENJ0_CROPO Unreviewed; 861 AA.
AC A0A7M4ENJ0;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
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 Name=LARS2 {ECO:0000313|Ensembl:ENSCPRP00005011653.1};
OS Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Longirostres; Crocodylidae;
OC Crocodylus.
OX NCBI_TaxID=8502 {ECO:0000313|Ensembl:ENSCPRP00005011653.1, ECO:0000313|Proteomes:UP000594220};
RN [1] {ECO:0000313|Ensembl:ENSCPRP00005011653.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCPRP00005011653.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; 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:ARBA00047469};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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DR AlphaFoldDB; A0A7M4ENJ0; -.
DR Ensembl; ENSCPRT00005013736.1; ENSCPRP00005011653.1; ENSCPRG00005008290.1.
DR GeneTree; ENSGT00390000015114; -.
DR Proteomes; UP000594220; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 GO; GO:0032543; P:mitochondrial translation; IEA:TreeGrafter.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR FunFam; 1.10.730.10:FF:000011; Leucine--tRNA ligase chloroplastic/mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000612; Leucyl-tRNA synthetase 2, mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000100; probable leucine--tRNA ligase, mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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 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; 3.
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.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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:UP000594220}.
FT DOMAIN 105..216
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 228..386
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 401..559
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 596..636
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 684..817
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 861 AA; 98229 MW; 42A0E693F278F982 CRC64;
MQPVWKRFGV SSSSLKRQLT GFRGLIKWQK TLAPGCIRSI YSETGKWESN YTRETRKRVE
KWWFPRIKEQ FCKISETDVI NPMGWDAFGL PAENAAVDHG LHPVTWTQSN IRHMKEQLNG
LGLSFSWEQE ITTCLPDYYK WTQYLFIKLF EAQLVYQKEA LVNWDPVDQT VLANEQVDEN
GCSWRSGAKV EKKYLKQWFI KTTSYAKAML DALSDLPDWY GIKEMQANWI GDSVGCYLDF
MLKVDGKVTG EKLAAYTYTP EAIYGASHIY ILPDHRLLHG NSSLKEVFQR EFIPGKDSLT
SVTAVNLLTN QEIPVVISAK SDFQNSLDTK IGIPSTNPED AAVAQNLGLP FTEVLEVLPD
GLEKVINSGE FTGMTRQEAL KALTQQARSK EVGGDLTSDK LRDWLISRQR YWGTPIPIVH
CQTCGSVPVP YEDLPVVLPN VTTFTGKGIS LLQTVPEWMN CLCPRCKGPA KRETDTMDTF
VDSAWYYLRY TDPHNCDRPF NKDLADYWMP VDLYIGGKEH AVLHLYYARF FSHFCHDQKM
TKTKEPFHKL LVQGLIKSET FRLTTTGQYL KREEIDLTET GPVHVKTKEK VQVTWEKMSK
SKLNGIDPEK FVQQYGIDTM RLFILFAASP EQDILWNVKT DAIPGVQRWQ IRLWSLATNL
IKARASGTLP NPELLSKNDK AEARKIWENK NLTISEVTND FTKNYMLNAA VSRLMSLSNT
LLQASQPLML HSVEFEEALA TLCIMLAPMA PHIASELWKG LVHVQNKLCT RYNWDADVLQ
QSWPKVDPEY LQQPDILEMS VLINNKACGK VNIPHQAAQN AEEVHELVLQ SELGAKLLKG
RTVKKAYLSP RTALVNFLVQ E
//
