ID   A0A2U3YC86_LEPWE        Unreviewed;       664 AA.
AC   A0A2U3YC86;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN   Name=LARS2 {ECO:0000313|RefSeq:XP_006741345.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006741345.1};
RN   [1] {ECO:0000313|RefSeq:XP_006741345.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006741345.1};
RG   RefSeq;
RL   Submitted (NOV-2023) 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, ECO:0000256|RuleBase:RU363035}.
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DR   RefSeq; XP_006741345.1; XM_006741282.2.
DR   AlphaFoldDB; A0A2U3YC86; -.
DR   STRING; 9713.A0A2U3YC86; -.
DR   GeneID; 102729252; -.
DR   KEGG; lww:102729252; -.
DR   CTD; 23395; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000245341; Unplaced.
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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
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; 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; 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.
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:UP000245341}.
FT   DOMAIN          62..256
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          271..334
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          399..439
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          489..610
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   664 AA;  75387 MW;  8A6B494FEC2C1910 CRC64;
     MASAWRRLGF YVSFLKSQRD GGPGIISRGR RVIPGWARDI YSATGEWTKE YTLQTRKEVE
     KWWHHRIKEQ ASKISEADKS KPKFYVLSMF PYPSGKLHMG HVRVYTISDT ISRFQKMRGM
     QVINPMGWDA FGLPAENAAI ERNLHPESWT QSNIEHMRKQ LDRLGLCFSW DREITTCLPD
     YYKWTQYLFI KLYEAGLAYQ KEALVNWDPV DHTVLANEQV DERGCSWRSG AKVEQKYLRQ
     WFIKTTAYAK AMQEALVDLP EWYGIKGMQA HWIGDCVGCH LDFTLKVDGQ VTGEKLTAYT
     ATPEAIYGTS HVAISPSHRL LHGHSSLKET FRKALVPGKD KPTAAKNREP FHKLLAQGLI
     KGQTFRRPSG QYLQREEVDL TGAVPVHAET KERLEVTWEK MSKSKHNGVD PEEVVEQYGI
     DTIRLYILFA APPEKDILWD VKTDALPGVL RWQQRLWALV TRFIEARAPG TAPQPQLLSD
     EERAESKKLW EYKNSVISEV TAHFTEDFSL NSVISQLMGL SSALLQASQR VVLHSPEFED
     ALCALTVMAS PMAPHITSEL WAGLAQVPGK LCAHYAWDAG VLLQAWPAVD PQFLQQPDVV
     EMAVLINNKA CGKIPVPQGV ARDQDKVHEL VLQSELGVQL LQGRSIKKAF LSPRTALINF
     LVQD
//