ID A0A0V1BMS5_TRISP Unreviewed; 1187 AA.
AC A0A0V1BMS5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:KRY38304.1};
GN ORFNames=T01_6605 {ECO:0000313|EMBL:KRY38304.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY38304.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY38304.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY38304.1};
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:KRY38304.1}.
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DR EMBL; JYDH01000026; KRY38304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BMS5; -.
DR STRING; 6334.A0A0V1BMS5; -.
DR eggNOG; KOG0437; Eukaryota.
DR InParanoid; A0A0V1BMS5; -.
DR Proteomes; UP000054776; 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:UP000054776}.
FT DOMAIN 19..99
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..920
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1187 AA; 135366 MW; 12E7F1B9E59A9CFC CRC64;
MDTRGRTKVA ELLKMEKDVQ KVWEEEKIYE MDAPEELDKA KFIATFPFPY MNGFLHLGHA
FSLTKCEFAV RYQRLRGKNA LFPFGLHCTG MPIKASADKL KAEIEEFGLP PNFPPDSELL
PDQSLLPETN SESTIKDKAK GKKSKAVAKS GALKYQWSIM KSLGFQDDEI AKFSDSLYWI
QFFPPVTVEH LKKMGLGIDW RRTFITTDVN PYFDSFVRWQ FLKLKERKRI DFGKRYTVFS
PKDGQPCMDH DRSSGEGVGP QEYTLIKLHL LEPYPKAIQT ICKGKRVYLV AATLRPETMY
GQTNCWVGPD IKYVAFTVNN DQDVFVCTRR AARNMAYQGF TVQEGQVNVL AEFFGKILFL
PTYEIVGCRV KAPLTVYESV YILPMMTVKS DKGTGVVTSV PSDSPDDYAA LQDLKNKKLL
REKFGIVDEM VLPFNPIPII DVPEFGKLSA PTACDEAKVQ SQNDIATLVA IKDKLYLKSF
YDGVSILLVG KYAGRRVQDV KKHIQKEMVE 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 SIVHAKWPTV
EPVVEELSKQ CAFLEDALHD FRIRYKSAMA SKQKKAGKMP VEKPNMAIIY VAAGYPPWQE
LTLTTLAKMH EVACGSLPEN KILSKELLKI EELKKHAKKL MPFVASVKES YDQKGVEAFS
LQAQVDELDI LTRNAAYLVS TLQLQAIQIH TSVHGGEKVQ EECRPGKPFI IFQTEKVCKL
ILINPTVGSG YFEFETAVLH GETVNNLKQR IAKRISVSDA KQILLYRYSD SVFGSRMIPV
LENFQQCTEV RSDGVFEVDN QRQPATLSLN EDGYHHPIGT QMIYVVV
//
