ID   A0A2Y9SUY4_PHYMC        Unreviewed;       903 AA.
AC   A0A2Y9SUY4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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_023979589.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023979589.1};
RN   [1] {ECO:0000313|RefSeq:XP_023979589.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023979589.1};
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_023979589.1; XM_024123821.3.
DR   AlphaFoldDB; A0A2Y9SUY4; -.
DR   STRING; 9755.ENSPCTP00005015995; -.
DR   Ensembl; ENSPCTT00005017654; ENSPCTP00005015995; ENSPCTG00005011271.
DR   KEGG; pcad:102995568; -.
DR   InParanoid; A0A2Y9SUY4; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000248484; Chromosome 18.
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:Ensembl.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   NCBIfam; TIGR00396; leuS_bact; 1.
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; 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.
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:UP000248484}.
FT   DOMAIN          61..257
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          271..400
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          444..600
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          638..678
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          728..852
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   903 AA;  102174 MW;  4B75E7000D1AB2E4 CRC64;
     MAPSWQRLSL YASLLKRQLN DGPDVIKWGR RVIPGCSRGI YSATGKWTKE YTLQTRKDVE
     KWWHQRIKEQ SSKISEADKS KPKFYVLSMF PYPSGKLHMG HVRVYTISDT IARFQKMRGM
     QVINPMGWDA FGLPAENAAI KRNLHPESWT QSNIRHMRKQ LDRLGLCFSW DREITTCLPD
     YYKWTQYLFI KLYEAGLAYQ KEALVNWDPV DQTVLANEQV DERGCSWRSG AKVEQKYLRQ
     WFIKTTAYAK PMQDALADLP EWYGIKGMQA HWIGDCVGCH LDFTLKVDGQ VTGEKLSAYT
     ATPEAIYGTS HVTISPSHRL LHGHSSLKEA FRKSLIPGKD CLTPVTAVNM LTQQEVPVVI
     LAKADFEGSL DAKIGIPSTS LEDTVLAQTL GLSYSEVIET MPDGTERLRS SAEFTGMNRP
     DAFLALTQKA RRKRVGGEVT SVKLKDWLIS RQRYWGTPIP MVHCPACGPV PVPLEDLPVT
     LPSITSFTGK GGSPLASASE WVNCSCPRCK GAATRETDTM DTFVDSAWYY FRYTDPQNTQ
     SPFSTALADY WMPVDLYIGG KEHAVMHLFY ARFFSHFCHD QKMVKHREPF HKLLAQGLVK
     GQTFRLPSGQ YLQREEVDLT GSVPVHANTR EKLEVTWEKM SKSKHNGVDP EDVVEQYGID
     TIRLYILFAA PSEKDILWDV KTDALPGVLR WQQRLWSLAT RFIEARVSGK VPRPQLLSNE
     EKAEGRKLWE YKNSIISQVT AHFTEDFSLN SAISQLMGLS NALLQASQRV VLHSPEFEDA
     LCALMVMAAP MAPLITSELW AGLALVPRKL CTHYAWDTSV LLQAWPAVDP QFLQQPDVVQ
     MAVLINNKAC GKIPVPQQVA QDQDKVHELV LQSELGVRLL QGRSIKKAFL SPRTALINFL
     VQE
//