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Database: UniProt
Entry: A0A3Q2DDZ0_CYPVA
LinkDB: A0A3Q2DDZ0_CYPVA
Original site: A0A3Q2DDZ0_CYPVA 
ID   A0A3Q2DDZ0_CYPVA        Unreviewed;       904 AA.
AC   A0A3Q2DDZ0;
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};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000016799.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000016799.1}
RP   IDENTIFICATION.
RG   Ensembl;
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_015236218.1; XM_015380732.1.
DR   AlphaFoldDB; A0A3Q2DDZ0; -.
DR   STRING; 28743.ENSCVAP00000016799; -.
DR   Ensembl; ENSCVAT00000025291.1; ENSCVAP00000016799.1; ENSCVAG00000019899.1.
DR   GeneID; 107088511; -.
DR   KEGG; cvg:107088511; -.
DR   CTD; 23395; -.
DR   GeneTree; ENSGT00390000015114; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000265020; 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; 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:UP000265020}.
FT   DOMAIN          72..263
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          272..431
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          445..601
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          639..678
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          727..838
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   904 AA;  102467 MW;  842FAD79F0926932 CRC64;
     MQASVRRLSL VSLSAVQTCQ NSTTLLSSAL RFLPPSIRTI FSETGVWDKD YRTENRRRVE
     EWWHPRIMKQ WQKDALDTDS NRKKFYVLSM FPYPSGRLHM GHVRVYTISD TIGHFQRMRG
     HQVLNPMGWD AFGLPAENAA IERGLDPEEW TKSNIQSMRE QLDSLGLCFN WDREITTCLP
     DYYKWTQYLF IKLFEAGLAY QKEAVVNWDP VDQTVLADEQ VDENGRSWRS GALVEQKLLT
     QWFIKTTNYA KPLLDALDDV PEWYGVKAMQ ANWIGECTGC YFDFTLKVDG KETGETLSAY
     SSSPEMVYGA AYLAILPSHR LLHGSSSVRS ALQRAFQPGR DSLTQVTAHN LFTGHEVPVV
     ISRKEAFDDY LDTVIGIPDS SEEDQSVARA LNLTWTTVLK THKDGTETLM NSQEFSDLTR
     EQAFHSITQK ARELGVGGHL TSSKLRDWLI SRQRYWGTPI PVVHCESCGA VAVPEEELPV
     TLPKAASLTG KGASPLGAVH DWVNCKCPRC KGPARRETDT MDTFVDSAWY YFRYTDPHNT
     DRPFRRHLAD HWLPVDVYIG GKEHAVMHLY YARFLCHFCK DQGLVAHREP FWKLLVQGLI
     KGQTFKLADS GQYLKREEID FQGKEPVALS GGSVEVTFEK MSKSKHNGLD PQEVVQQYGV
     DTVRLYILYA APPEQDILWN VKTDALPGVL RWQSRLWQLV TKLRGARQLG DVPNPSLLKK
     KELAEVRKIW ENKNYAVQEV TTHFTEDFLF NAALSRLMGL TNTLSSATVR VLQHSVEFEE
     ALAALVIMAA PMAPHLASEL WAGLCSVKNP LSPLLLRGGD VLQQPWPIVD TEYLEAPDFV
     ELSVLINNKP CGTVTIPLQV SKDSSRVQQL VLESPIGQKL LSERSIKRAI LSPRTALINF
     LVDE
//
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