SYL_MYCGA
ID SYL_MYCGA Reviewed; 805 AA.
AC Q7NB47;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=MYCGA4330;
GN ORFNames=MGA_0087;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; AE015450; AAP56783.1; -; Genomic_DNA.
DR RefSeq; WP_011113683.1; NC_004829.2.
DR AlphaFoldDB; Q7NB47; -.
DR SMR; Q7NB47; -.
DR PRIDE; Q7NB47; -.
DR KEGG; mga:MGA_0087; -.
DR PATRIC; fig|233150.7.peg.491; -.
DR HOGENOM; CLU_004427_0_0_14; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001418; 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 Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..805
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152044"
FT MOTIF 39..50
FT /note="'HIGH' region"
FT MOTIF 583..587
FT /note="'KMSKS' region"
FT BINDING 586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 805 AA; 94221 MW; A959DB38B8888710 CRC64;
MYNHNLIEKK WAKIWNDQKI YSFQIDKNKP KYYILDMFPY PSGKGLHVGH VKAYMATDVI
SRWKNALGFN VLHPIGWDAF GLPAEQYAIQ TNNHPAKFTQ ENINNFRTQL KRLGFNYDYR
LEVDTTNKNY FKWTQWIFKK LYEHDLAYQA DIEVNWCEQL GTVLANEEVL TDENGNKISE
RGSYPVIKKK MRQWVLKITA FADQLIDDLE NLNWPNSIKA MQVNWINKSV GASIKFEIDQ
LDNQTIEVFS SRADTLFGAS FLALSFDHPL VKQKLITDKN NAIEQFIKDN SIDQRVRYQG
INTNYFAIHP ITKKKIPIYL ADYILSDYGT GAVMGVPAHD ERDYQFAKQY DLEIIPVIKA
DQYPYLLDGE HINSEFNNGL NNEQAIQKTI AYLREHNLGD QKINYKLRDW IFSRQRYWGE
PFPVLFDEED NIYLLKDSEL PVELPQLSDF SPNKDGLPPL ANADDQWLHP IIDQKKYRRE
INTMPQWAGS CWYYLAYLLK LTDLNQADGD QNYLALNSEK AKELFDHFMP VDLYVGGQEH
AVLHLLYARF WYKFLHHIKI VSSTEPFSQL INQGMILGED NTKMSKSKGN IINPDDLVLS
HGADTIRTYV MFMGPLNASL AWNSNALNGT RKFLERVYNL FDRVEINDSI NQNLNYDYHN
FLKKINKHLE NFEFNLVVSE MMIFINACYK QTQVNKEMIT NFLIVLSFFA PYLAEELNSK
LNNPTLLYKM RLAQWDEAYL VKNTTTISCS INGKFKLVHE FDLDSDEQEV ANYFLNQDLI
KRNLENKKLV KTIFVKNKVI NFIIK
