ID J3TYS7_9ENTR Unreviewed; 863 AA.
AC J3TYS7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=A35E_00269 {ECO:0000313|EMBL:AFP85575.1};
OS secondary endosymbiont of Heteropsylla cubana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts.
OX NCBI_TaxID=134287 {ECO:0000313|EMBL:AFP85575.1, ECO:0000313|Proteomes:UP000003937};
RN [1] {ECO:0000313|EMBL:AFP85575.1, ECO:0000313|Proteomes:UP000003937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hcub_S {ECO:0000313|EMBL:AFP85575.1};
RX PubMed=22821013; DOI=10.1093/molbev/mss180;
RA Sloan D.B., Moran N.A.;
RT "Genome reduction and co-evolution between the primary and secondary
RT bacterial symbionts of psyllids.";
RL Mol. Biol. Evol. 29:3781-3792(2012).
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, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CP003547; AFP85575.1; -; Genomic_DNA.
DR RefSeq; WP_014888872.1; NC_018420.1.
DR AlphaFoldDB; J3TYS7; -.
DR STRING; 134287.A35E_00269; -.
DR KEGG; sehc:A35E_00269; -.
DR PATRIC; fig|134287.3.peg.260; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000003937; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 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; 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; TIGR00396; leuS_bact; 1.
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 Pfam; PF09334; tRNA-synt_1g; 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 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|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000003937}.
FT DOMAIN 39..182
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..406
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 420..575
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 621..654
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 703..825
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 622..626
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 863 AA; 99586 MW; C4A9642A89B7F9AE CRC64;
MQETYSPEEI ELKVQQHWDR QDTFKVTEER DKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
VIARHQRMLG KNVLQPIGWD AFGLPAEGAA IKNKIAPACW TYSNIDYMKK QLKRLGFSFD
WSREITTCRP EYYRWEQWFF TCLYNKGLVY KKTSLVNWCP QDNTVLANEQ VINGFCWRCD
TKVDKKEIPQ WFVKITAYAD QLLSDLDTLE DWPEKVKTMQ RNWIGYTEGA EITFQLLDRK
EKLTLYTTRP DTLMGITYLA IPLSHTLSLQ AATDNIALKN FIQKSSLSNF TNIEDMQKNN
LKKQGMATGL YALHPLTNAI LPIWMSNYMV KDDFSYAVMG VPGHNQCDFE FARKYNLPVK
AVIRNDDGSE PDLSLRAMTK KGILFNSGIF DGLDFQEAFN AVIDVLSSCG VGEKKTYYRL
RDWCISRQRY WGAPIPMITL IDGTVKPIPD DQLPVILPED VVIDGISNPL NNDLEWIKTS
DNGEIAFRET DTFDTFMESS WYYARYTCPD YNFGMLDPEA ANYWLPVDQY IGGVEHAILH
LMYFRFYHKL LRDQGLVTSS EPAQRLLCQG MVLADTFYDL TDQGERVWIS PSDVRVERDK
KGKIIKAIDS KGNALVYAGI SKMSKSKNNG IDPQDMVKKY GADTVRLFIM FAASPELNLE
WQESGIEGVN RFLKRIWRFV YDHHRKGPFQ LLDIISLNYE QKSLRRDIHK TIVKVTEDIG
RRRMFNTAIA SIMELMNQLV RFPSKGAQNL ALLHEAMLVI VRLLYPFTPH ICFILWNVLG
GEGNIDHASW PVADKAAIVE EHNVVIVQIN GKLRGKIIVP KDADEALIRR HAFRESFVEK
HLEGSTVRKM IYIPGKLLNL VLD
//
