ID   A0A3Q3AP77_KRYMA        Unreviewed;      1185 AA.
AC   A0A3Q3AP77;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=LARS1 {ECO:0000313|Ensembl:ENSKMAP00000013269.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000013269.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000013269.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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_017276725.1; XM_017421236.1.
DR   AlphaFoldDB; A0A3Q3AP77; -.
DR   STRING; 37003.ENSKMAP00000013269; -.
DR   Ensembl; ENSKMAT00000013472.1; ENSKMAP00000013269.1; ENSKMAG00000009903.1.
DR   GeneID; 108238882; -.
DR   KEGG; kmr:108238882; -.
DR   CTD; 51520; -.
DR   GeneTree; ENSGT00390000012163; -.
DR   OMA; KFIEWQF; -.
DR   OrthoDB; 5472610at2759; -.
DR   Proteomes; UP000264800; 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; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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:UP000264800}.
FT   DOMAIN          20..104
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          182..764
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          803..915
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          113..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  135414 MW;  3376BD08F8F14A6F CRC64;
     MTERKGTAKL DYLRKIELEI QEKWEKEKAF ESDAPSTVGE SSNKNKYFVT FPYPYMNGRL
     HLGHTFSLSK CEFAVGYQSL KGKKCLFPFG LHCTGMPIKA CADKLKREME LYGNPPQFPE
     EEEEEEKEKP KMSDEIIIKD KAKGKKSKAV AKSGSSTFQW DIMRSLGLND QEISKFASAE
     HWLEYFPPLA VKDLKQMGVK VDWRRSFITT DVNPFYDSFV RWHFVTLKER KKIKFGKRYT
     IYSPKDGQPC MDHDRQTGEG VGPQEYTLIK MKIVEPYTAK FKSKVFYSSG MKGKTIFLVA
     ATLRPETMFG QTNCWVRPDM KYVAFETTSG DVFISTSRSA RNMSFQGFTK ENGVVPVVME
     ILGQDILGCA LSAPLTSYKI IYALPMLTIK EDKGTGVVTS VPSDAPDDIA ALRDIKKKQA
     LREKYGIEDK MVLPFEPVPI IEIPGYGNLS APLVCDELKI QSQNDKEKLA EAKEKVYLKG
     FYEGIMLVDG YKGQKVQDVK KPIQKMMVER GEAMIYMEPE KQVMSRSADE CVVALCDQWY
     LDYGDSEWKQ QANEVLKSLE TFCEETRRNF EATLAWLQEH ACSRTYGLGT RLPWDEQWLI
     ESLSDSTIYM AYYTVAHLLQ GGVLNGQGAS PLDIKPEQMT REVWDFIFFK TSPFPKTDIP
     REHLQRLRRE FEYWYPVDVR VSGKDLVPNH LSYYLYNHVA IWPKDSGKWP QAVRANGHLL
     LNSEKMSKST GNFLTLCQAI EKFSADGMRL ALADAGDTVE DANFVETMAD AGILRLYTWV
     EWVKEMIANQ NNLRTGPSDT FNDRVFASEM NAGIMKTEQH YERMMYKEAL KSGFFEFQAA
     KDKYRELAIE GMHRELVFQF IERQMLLLAP ICPHLCEYTW GLLGKTGSLM KASWPAAGPV
     DEVLIRSSQY LMETAHDLRL RLKAYMLPPK NKKGDSKPPA KPSHCNIYVA KSYPPWQHSA
     LSLLGKHYKS NNRVLPDNKV IASELGALPE LKKYMKRVMP FVAMIKENLE KNGPRVLDLE
     LEFDERTVLM ENLVYLTNSL ELEQIDVLFA SEADDKVKED CCPGKPFSVF RSEPGVSVFL
     INPQPYNGLF STKIDIRQGD NRDGIIRRLA KVNRLIKDLS RVKLMRYEDP ELGPRRVPVL
     GQEEQGKLPI SSKSVFNVNL QEKKVTLADN GLTVNIGDTL AYLIH
//