ID A0A0P7KCT5_9MOLU Unreviewed; 817 AA.
AC A0A0P7KCT5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ECO:0000313|EMBL:QLL36773.1};
GN ORFNames=EPWB_v2c1410 {ECO:0000313|EMBL:QLL36773.1};
OS 'Echinacea purpurea' witches'-broom phytoplasma.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrII (Peanut WB group).
OX NCBI_TaxID=1123738 {ECO:0000313|EMBL:QLL36773.1, ECO:0000313|Proteomes:UP000050566};
RN [1] {ECO:0000313|EMBL:QLL36773.1, ECO:0000313|Proteomes:UP000050566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCHU2014 {ECO:0000313|EMBL:QLL36773.1,
RC ECO:0000313|Proteomes:UP000050566};
RX PubMed=26607900;
RA Chang S.H., Cho S.T., Chen C.L., Yang J.Y., Kuo C.H.;
RT "Draft Genome Sequence of a 16SrII-A Subgroup Phytoplasma Associated with
RT Purple Coneflower (Echinacea purpurea) Witches' Broom Disease in Taiwan.";
RL Genome Announc. 3:e01398-e01315(2015).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; CP040925; QLL36773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7KCT5; -.
DR Proteomes; UP000050566; 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 Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 1.
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:UP000050566}.
FT DOMAIN 41..173
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 225..411
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 426..627
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 668..781
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 594..598
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 817 AA; 95852 MW; 1F2400238622D99E CRC64;
MLVYDFRSIE AKWQLHWDEQ QTFKTDIDYN KKKFYCLDMF PYPSAQGLHV GHLEGYSASD
IINRFFRMQG FNVLHPFGWD SFGLPTERYA AQTGQHPAYV TYQNIANFKK QIKSLGKGID
WSRELATSDS YYYKWTQWIF KKLYQNQLAV LQDVEVNFCP NLGTVLANEE VISTPEGIIS
ERGGHPVFKR KMKQWVLKIT KYADRLLNDL SLLDWPTSIK EMQIKWIGKT SGFIFYFPLL
MNNAQYLSVF TTMPQMIFGV SALILAPEHP WVSLLTTAEN QSNVNDYLSK TQRKSNLERD
INREITGVFT GSYAINPCNK QKIPIWISDY VFMHFGTGAL MSVPLYNQKD FVFATKYNLN
KYIIKYCSSC CHLYSEIKRI KKPCLQTSGT FINSDFLNGL DENLAKEKIM DLSIKNKWGE
PFNTYKIHDW LYSRQIYWGE PFPVYYDENN KIYLMSDHEL PLELPETDKI EYLYKSESPL
SQIDSWLYFC KNGKNYKRDS NTMPQFAGSS WYYIGYILKN YLSMIPINTM EAKKLLDYFL
PVDIYIGGAE HAHGHLIYAR FWCKCLYDWG LISTPEPFYK LINQGMILGN DNLKMSKSRG
NIVNASEVLD TYGADVIRLY IMFLGPLEEN KSWSGQGLKG IQRFLNRIYN IFDKFTICEQ
AFTSLNKITH QTIRNVTEYY NKFQFNKVIS QLMIMTNHIY QYEKVDRFQI RILLQLLNPI
APHITEELNQ IKLNSKEELV YSSWPKYNIS ILEEKETTII IQINGKMKSQ LLIPFDTDKS
EILKIVEKDE KILRFIKNKK IINTIYVKNK LLNIVLI
//
