ID I7B8X7_MYCHA Unreviewed; 707 AA.
AC I7B8X7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 Name=leuS {ECO:0000313|EMBL:AFO51700.1};
GN OrderedLocusNames=MHLP_00600 {ECO:0000313|EMBL:AFO51700.1};
OS Mycoplasma haematolamae (strain Purdue).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1212765 {ECO:0000313|EMBL:AFO51700.1, ECO:0000313|Proteomes:UP000006502};
RN [1] {ECO:0000313|EMBL:AFO51700.1, ECO:0000313|Proteomes:UP000006502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Purdue {ECO:0000313|EMBL:AFO51700.1,
RC ECO:0000313|Proteomes:UP000006502};
RX PubMed=23105057; DOI=10.1128/JB.01557-12;
RA Guimaraes A.M., Toth B., Santos A.P., do Nascimento N.C., Kritchevsky J.E.,
RA Messick J.B.;
RT "Genome Sequence of "Candidatus Mycoplasma haemolamae" Strain Purdue, a Red
RT Blood Cell Pathogen of Alpacas (Vicugna pacos) and Llamas (Lama glama).";
RL J. Bacteriol. 194:6312-6313(2012).
RN [2] {ECO:0000313|Proteomes:UP000006502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Purdue {ECO:0000313|Proteomes:UP000006502};
RA Guimaraes A.M.S., Toth B., Santos A.P., Nascimento N.C., Sojka J.E.,
RA Messick J.B.;
RT "Complete genome sequence of 'Candidatus Mycoplasma haemolamae'.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003731; AFO51700.1; -; Genomic_DNA.
DR AlphaFoldDB; I7B8X7; -.
DR STRING; 1212765.MHLP_00600; -.
DR KEGG; mhl:MHLP_00600; -.
DR PATRIC; fig|1212765.3.peg.144; -.
DR HOGENOM; CLU_004427_0_0_14; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000006502; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 3.10.20.590; -; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
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; 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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000006502}.
FT DOMAIN 2..133
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 307..510
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 556..665
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 707 AA; 82891 MW; 53D9072B4BFCA43A CRC64;
MFPYPSGAGL HIGHVKGYLA TDIIARYKKM KGFSVLHPIG WDAFGLPAEQ FAIQNKSDPN
VFTQKNISSF RDELKSLFFS YDFNREIDST DPNYYAITQQ IFLKLYDRGL ASLEAKTVNW
VDELHTVLAN EEIYKGEDGR YYSERGDYPV RKRKLTQWVL KITKFAEELN RDLKHLDWSD
RIKAIQSEWI GEYEAFKFTL KINGREFNHY EREVDAIRSI VGFYIFKDSE IYKALNIKHQ
PKEGEILLEY SDSQTIDKLK LVYRELGEAQ REDETGLTPI YEDLVGDRRI PSFINWKVLP
KVKRFKLQDW VFSRQRYWGE PIPLYYDSEG RIYKEEELPL RLPSYRSSSQ LREERPNTST
TLEEEIATPL SYYTDWVHER EGYRRDTNTM PNWAASSWYF LAYLLRTNDG YLPLDSKAAR
ELIERWMPVD LYVGGQEHAT MHLIYARFWY KAICSFLGIK GQQEPFQHLV NQGMILGEDG
KKMSKSKGNC ISISQLLKDH GGDSIRLSVA FLGPLELTQY WDTRQLSVFE SWIERIYSYF
LSVSSSLSKE TKENYKLGEF LSKVESSINS FKFNVLVSEL MVFFRYLKEK KEKELEEHRG
FIQILSYLAP AISEEIWIEL LKEQESVYLS SWIAISKNKK KEVIYSIQLN NKHKLSIPLS
SSLETSEEIF ESLSKTEDYQ SLMKDKELKK YIVVPGKVIN LIAVLKS
//
