ID A0A0R3QL11_9BILA Unreviewed; 883 AA.
AC A0A0R3QL11;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ORFNames=BTMF_LOCUS6413 {ECO:0000313|EMBL:VDO21712.1};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000836201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0000836201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO21712.1, ECO:0000313|Proteomes:UP000280834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; UZAG01015589; VDO21712.1; -; Genomic_DNA.
DR STRING; 42155.A0A0R3QL11; -.
DR WBParaSite; BTMF_0000836201-mRNA-1; BTMF_0000836201-mRNA-1; BTMF_0000836201.
DR Proteomes; UP000050602; Unplaced.
DR Proteomes; UP000280834; 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; 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; 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:UP000280834}.
FT DOMAIN 51..241
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 408..552
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
SQ SEQUENCE 883 AA; 101970 MW; A380EAC45E8F517F CRC64;
MESSFLLPKI RYHLAKFYSK ASASHIKTPM LIWPRKEYGI STKLFDLEKY WKEVAQIAPS
IHFSRPKKYI LSMYPYPSGR LHMGHMRVYT ISDVLARYYR LNGYNVIHPI GWDAFGLPAE
NAAREVGVDP AQWTANNIDV MRQQLLSTGI IFDWNREIST CSPDYYRWTQ WIFCRLFERG
LVRRALTEVH WDPIDCTVLA AEQIDAEGRS WRSGAVAEKR KIKHWMIETP KYAKRMYVGL
EKLAHWKEVA AIQANWIGKC DVWRFLLPLK ERNGTVLDEK FDLRIREPHH LATASVIFIQ
FGHPLFSLAD EKEEIGVLKV TALNIITGKD MHIIYMNENA AKNRNGFILN ARLPCEADEF
DKKVTESFGF STERCRFSLT NNDIIQIAEI FPFKFGDYGG YETSERLLDW VVSRQRKWGT
PIPVLLSADD RCAAIVADDQ LPVIAAHYKY DEKIPCQRLP DGFGYLEKDT LDTFFDSSWY
YLRFLDPKND IELVSEKKSI DMPVDVYVGG IEHAALHLFF ARFVSYFLHD IGVSSVQEPF
DSLLPQGIVC SRTFKRSDSG KYLKEDDVVQ TGNGFIAKKD GCAVFTQFEK MSKSKHNGVD
PLSVLKLKGI DLTRLQLLNE AAPREPINWG DTELKGLFKF MERTSDVISF YVEQHALSAS
TLPEPLDIAR EEKYRTIYNF YVRNISMVIE VLHLHNTAID HLQSFVKFLK KSSAEAYRCS
VQLERCVHAL VIMMQLFTPH LAAEYWAALR SVPALSGHRV WLDKEINEQP WPQVDPDAKI
DFMINVGKLS CGRVEVPRLE IEHLSSEEVL QYAIDDVHSI FFQELASLGF RPISCKKLSR
TGFYVLLEVK FNKVPAEETL IDILKQTRMQ RLKVKRARKK AEK
//