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
//