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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//