ID A0A384LGW1_PLAKH Unreviewed; 1291 AA.
AC A0A384LGW1; A0A1A7W1W4; B3L108;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 33.
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=PKNH_1322300 {ECO:0000313|EMBL:CAA9990261.1};
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAA9990261.1, ECO:0000313|Proteomes:UP000031513};
RN [1] {ECO:0000313|EMBL:CAA9990261.1, ECO:0000313|Proteomes:UP000031513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H {ECO:0000313|EMBL:CAA9990261.1,
RC ECO:0000313|Proteomes:UP000031513};
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D.,
RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S.,
RA Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M.,
RA Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S.,
RA Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A.,
RA Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W.,
RA Newbold C.I., Barrell B.G., Berriman M.;
RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite
RT with host range from monkey to man.";
RL Nature 455:799-803(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; 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:ARBA00047469};
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; AM910995; CAA9990261.1; -; Genomic_DNA.
DR RefSeq; XP_002258040.1; XM_002258004.1.
DR FunCoup; A0A384LGW1; 284.
DR STRING; 5851.A0A384LGW1; -.
DR GeneID; 7319402; -.
DR KEGG; pkn:PKNH_1322300; -.
DR VEuPathDB; PlasmoDB:PKNH_1322300; -.
DR InParanoid; A0A384LGW1; -.
DR OMA; KRECDIM; -.
DR OrthoDB; 15954at2759; -.
DR Proteomes; UP000031513; Chromosome 13.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 GO; GO:0032543; P:mitochondrial translation; IEA:TreeGrafter.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 2.
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; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
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 InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
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:UP000031513};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1291
FT /note="leucine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030070915"
FT DOMAIN 143..344
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 479..564
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 921..959
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 1103..1199
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 817..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 150954 MW; 50B209C2CCA76830 CRC64;
MPLSWTLTLI LCYLLLCETI HHVFAVRSEN VGCPVRGASA GCSVIGVRAG YVAPSLHPSE
CAWRRARRDT KLWAYNFRAI ERKWQVVWNS KRLLDRDFAR FNRNAQAESQ GEGEKLAKGS
KVSKVGRVGK GEWKNEESVG REFEEEERRK TTRRKFYILD MFPYPSAQGL HMGHILCFTI
TDVLAKFKRM TNHCVFHPIG WDSFGLPCDR MSMKLKVDPR EIIQKNILNF KEQVIKMGFL
FNWDNEINTS DEIFYKWTQW IFIQMYLKKL GYKKNSYVNW SKEIKCVISN DEMKNEANVE
GLKVTKRKLL QWYLRITKYA TRLIEDLKEI DWPEKIKRMQ INWIGKKKGI ILKAKVIPIH
EWKTRQISHT PSGCSIPHVL YHSIYENDEM TLLLNYLYHT GGYGYDFFYS FVRMGGEKYP
IEWVENQMER LIQEEDAVEN SLRRIKPSVP KPVLPPNKGE KKYLLNFDTD KEENEGGDLY
VKIFLNEKEA IFPGDKLVVS VNHPKIDKIV NGKKCLLNFV RRGIRENDTE RLKNEQIFFT
GSVIYNPIIG KYIPIYVCTY VLENNSDLLF VKRGRREKVE ETSKGEEALH KLLSSSRYSK
KYSVYNLKDW LFSRQRYWGE PFPFLFPVGG TKEGGQEKGE IKNVCNSPVE GIYIDDIPVH
LPKFHKRVYE LGSNRYNEGS PSVLSRFKNW VFQRRGNVLY KRECDIMPQW AGSSWYFLRY
LDSKNSNCIF NKERANLWMP VDLYVGGSEH AVLHLLYARF FHKFLYDLKL VKHKEPFQRL
FNQGLLLSAS SFFAYTTLEG KLVSYAAVRA EAAEGDKIEK EGGTQQRQGS VESNITESNP
GDDVLIGGNG EPLKEKQIYP SGAELSSDKQ NCSIEKALGE KVSCENEKYR KYRIPEELVV
QREGKYFLKD TPDVEVKANY EKMSKSRGNT VNPNDIVKKY GSDCLRLYIL FLGPIDQNKK
WDLKGIKGTF KFLTNLYNLF VKDTSLAGEK RQEEGSTTTE VDSGEIPQEG GDSVVEPPRK
RNSEHIICTK CRRKKRNQHM ILNFEMIKSG GYKLEGKFNP DEKKEAIKRN INFLRSEDHS
CKELSDFIVK KKVQDIETEK KERANFFINK ITKCLNNMKL NTAVSFFMIF FNEIKKWDYI
PLKIFLVFVK LLFPFCPHIC EEFWFFYLKK YKAERKQICY FCNSSLMYFA RWPSLFELES
AKVSRLSIRL NNRHVTFMEV ARESGLEELR SVESCEHSER PTNGEPSERS EKIIREATNK
ITDRIEKEKK KGKRLVNVMY IPNKVVNFVF K
//
