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Database: UniProt
Entry: U4UJX5_DENPD
LinkDB: U4UJX5_DENPD
Original site: U4UJX5_DENPD 
ID   U4UJX5_DENPD            Unreviewed;       814 AA.
AC   U4UJX5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=D910_11644 {ECO:0000313|EMBL:ERL94364.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL94364.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL94364.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
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   EMBL; KB632387; ERL94364.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4UJX5; -.
DR   STRING; 77166.U4UJX5; -.
DR   Proteomes; UP000030742; 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; 2.20.28.290; -; 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:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 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:UP000030742}.
FT   DOMAIN          47..243
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          353..501
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          678..738
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   814 AA;  93278 MW;  F1A48A4A23FC59D0 CRC64;
     MRLPILAKET FALFARKKSP CPQRFLSGCG LWTEDLSPQV KQQIESHWRD KIGVKPPKTP
     TPTTKDKYYV LSMFPYPSGS LHMGHVRVYT ISDTIARYQR MNGRNVIHPI GWDAFGLPAE
     NAAIDRQLAP SDWTANNINH MKAQLKQLGC SFEWERELAT CDPEYYRWTQ DLFLKLYDAG
     LAYQKEALVN WDPVDQTVLA DEQVDENGLS WRSGAKVEKK LLKQWFIRTT KFAKQLYDGL
     DDAVLHDWRD IIKLQKHWIG NCDGVNFDFK VNSSCSSTSV ATFWTSTPEL IEEAKFVAVT
     SNHVLAKQEG VTSADGTVKL QSVVTNPFNK EQLPLYVTND IEFADETDSF IGKYWGTPIP
     IVHCKNCGPV PVPREKLPVE LPKLSQLSSK GKSPLEDVSE WVNTNCPQCN GEAKRETDTM
     DTFVDSSWYF LRYLDPQNSK QMFDKEKAFQ MTPVDLYIGG KEHAVLHLYY ARFVSHFLHS
     LGLLPEREPF KRLLVQGMVM GRSFRVKTTG QYLPEDQVKV IDLKKGKAVS KETGDPVTIS
     WEKMSKSKHN GVDPEEMFRE YGTDTTRLLI LADVAPTSHR NWNSNTFPGV LNWQRRLWIT
     VQDFIKHRTN PPAIAADEEF KNQEDYLWDS RNFYTKGVSF NYIVSQQMSV AVSKMQGLTN
     SLRRAPVAVF CHSRQFERAL AAQIILLAPM APHFASELWA GFTSAPNRLN QSTEILWDRP
     VLEQQWPETD MNYQLDLVCQ VNGWENCTVK FERRILDRLD KEEAVRVAMS QQAIESTLRM
     RNVLNVKFTV YPGVDSVVNF MTDQPPPKKK PVPV
//
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