ID A0A0V0SCT4_9BILA Unreviewed; 1187 AA.
AC A0A0V0SCT4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=Lars {ECO:0000313|EMBL:KRX24506.1};
GN ORFNames=T07_6018 {ECO:0000313|EMBL:KRX24506.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX24506.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX24506.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX24506.1};
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:KRX24506.1}.
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DR EMBL; JYDL01000017; KRX24506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0SCT4; -.
DR STRING; 6336.A0A0V0SCT4; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
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 Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
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:UP000054630}.
FT DOMAIN 19..100
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 670..769
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 811..922
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1187 AA; 135293 MW; 7C7CF4FE8F215DB1 CRC64;
MDTRGRTKVA ELLKMEKDVQ KVWEEEKIYE MDAPEELGKA KFIATFPFPY MNGFLHLGHA
FSLTKCEFAV RYQRLRGKNA LFPFGLHCTG MPIKASADKL KAEIEKFGLP PNFPPDSELL
PDQSLLPETN SESTIKDKAK GKKSKALAKS GALKYQWSIM KSLGFQDDEI AKFSDSLYWI
QFFPPVTVEH LKKMGLGIDW RRTFITTDVN PYFDSFVRWQ FLKLKEQKRI DFGKRYTVFS
PKDGQPCMDH DRSSGEGVGP QEYTLIKLHL LEPYPKAIQT ICKGKSVYLV AATLRPETMY
GQTNCWVGPD IKYVAFTVNN DQDVFVCTRR AARNMAYQGF TAQEGQVNVL AEFFGKILFL
PTYEIVGCRV KAPLTVYESV YILPMMTVKS DKGTGVVTSV PSDSPDDYAA LQDLKNKKLL
REKFGIVDEM VLPFNPVPII DVPEFGKLSA PTACDEAKVQ SQNDIATLVA IKDKLYLKSF
YDGVSILLVG KYAGRRVQDV KKHIQKEMIE TGDACIYYET EKPVISRSGD ECVVALCDQY
LNYGDHKWKE ATKKALQGLN TYTDNVYNNL NATVDWLHEH ACSRSYGLGT KLPWDEQYLI
ESLSDSTIYM AYYTVAHLLQ GGVFDGSKCG PLNIKPEQLT PAVWDYIFYD DQLYENVKTD
IEKWKLDKLK HEFNYWYPVD LRVSGKDLIQ NHLTYYLYNH VAMWPSDPSK WPRSVWANGH
LLLNNEKMSK STGNFLTLVE AVERYSADGM RLALADAGDS IEDANFMETM ADAGVLRLYN
FLTWVIESIT SLDEMANHPP STFPELIFQN DINKYVQISA ENYENMQFKE VVKSAFFEFQ
AARDRYREWS MMALNRNLIL RFIETQAIIL SPICPHICEA IWKLLGNVKN SIMHAKWPTV
EPVVEELSKQ CAFLEDALHD FRIRYKSTMA SKQKKAGKMP VEKPNMAIIY VAAGYPPWQE
LTLTTLAKMH EVACGSLPEN KILSKELLQI EELKKHAKKL MPFVASVKES YDQKGVEAFS
LQAQVDELDI LTRNAAYLVS TLQLQAIQIH TSVHGGEKVQ EECRPGKPFI IFQTEKVCKL
ILINPTVGSG YFEFETAVLH GETVNNLKQR IAKRISVSDA KQILLYRYSD SIFGSRMIPV
LENFQHCIEV RSDGVFEVDN QRQPATLSLN EDGYHHPIGT QMIYVVV
//
