ID   A0A0V0S3T7_9BILA        Unreviewed;       962 AA.
AC   A0A0V0S3T7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SNRK {ECO:0000313|EMBL:KRX21348.1};
GN   ORFNames=T07_3412 {ECO:0000313|EMBL:KRX21348.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX21348.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX21348.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX21348.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX21348.1}.
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DR   EMBL; JYDL01000040; KRX21348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0S3T7; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
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; 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; 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   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:UP000054630}.
FT   DOMAIN          124..322
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          469..629
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          751..859
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   962 AA;  109724 MW;  5670DF2F388948DA CRC64;
     MELIGFVECA EAQHLKIIRL FNVQKAFATS FSIIDLLEKE IRESSNSLST TAVCIADSDE
     VEELNGENGF VCGLLPNYSA QPVQKNGSPV CVVVGSVEGE LLTNLHIFGT KKKLSSEDIH
     CIEKHWHDKV VNYELSEKQQ SKGKKYILSM FPYPSGKLHM GHVRVYTISD CLARYNELRG
     YEVIHPMGWD AFGLPAENAA IERNLDPEVW TESNIAAMKK QLVELGCRFD WTREIATFKS
     QYYRWTQWLF LQLYKAGLVY QKRSYVNWDP VDCTVLADEQ IDERGCSWRS GAAVVQKPLL
     QWFVKTSFFA KALYDELDNL VSWQDVVDIQ RHWIGKCDSY RFKFKILNEN SGQETGDCVD
     IFVDCLQQLC SAKAVAISSK HICSDHSPTQ IKVLNSVTNQ LLPVFVTDHI DYVGSENARL
     VSADDSVYQK CGLSGESGLA ETRILLSDEQ ILERAKAADC GGYLTSRRLN DWVVSRQRFW
     GTPIPIVHCS NCKAVPVPES QLPVTLPTVH LFGSKGKLLP LHQYNDWLST VCPECGEPAR
     RECDTLDTFF DSSWYYLRFL DPQNDRQPFD SNIANQMMPV DIYIGGKEHA ALHLFYARFM
     CHFLRSIGFV ANAEPFSRLL TQGMVMAKTY KTEDTGEYIP SSSVIQSGSG YVEINSRRAV
     TESWEKMSKS KHNGIDPQNL LDNIGCDFTR LLITSNVSPQ SHRHWDTAGL KGVENWLNRV
     RYLVVTLISM RSFSNTESTS VLNVDEQKKT DEYLKENYNH FVREVTFHLE ETFLLNVAIS
     RLQGFTNSLR KCSPETIGFN VEFERCLRAL LVMIFPFAPN ISSELWSILN DSIRLSKSIS
     QTRTDGHVWN QPWPLVDKDA VVALSVYING MIAERIFMNW HALLSLEQNE AMRMALQSRN
     VAEKIGPATS VQLKGFYFEI GKASFCCSKE MKKLHFCNNN QKKEEVDDEE EEIYETLLFK
     RK
//