ID A0A1M6DFA9_MALRU Unreviewed; 851 AA.
AC A0A1M6DFA9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=SAMN02745165_00655 {ECO:0000313|EMBL:SHI71791.1};
OS Malonomonas rubra DSM 5091.
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Geopsychrobacteraceae; Malonomonas.
OX NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHI71791.1, ECO:0000313|Proteomes:UP000184171};
RN [1] {ECO:0000313|EMBL:SHI71791.1, ECO:0000313|Proteomes:UP000184171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5091 {ECO:0000313|EMBL:SHI71791.1,
RC ECO:0000313|Proteomes:UP000184171};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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, 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; FQZT01000002; SHI71791.1; -; Genomic_DNA.
DR RefSeq; WP_072905541.1; NZ_FQZT01000002.1.
DR AlphaFoldDB; A0A1M6DFA9; -.
DR STRING; 1122189.SAMN02745165_00655; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000184171; Unassembled WGS sequence.
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; 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; 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:UP000184171}.
FT DOMAIN 41..180
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..577
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 611..651
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 693..814
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 612..616
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 851 AA; 96703 MW; FF7F9D77B3A466D3 CRC64;
MEKQYIPKDV ERKWQEKWRQ DQAFRVTEDP SKEKYYLLEM FPYPSGRIHM GHVRNYAIGD
VVARFKRMQG FNVLHPMGWD AFGMPAENAA IENKTHPAKW TYENIDSMRQ QLERIGLSYD
WQREFATCHP DYYRWEQLVF LKMYEKGLAY KKGSSVNWCP DCATVLANEQ VEDGSCWRCH
NLVEQKELEQ WFFKITDYAD ELLDWTDKLP GWPERVLAMQ RNWIGKSYGC EIEFPVADSE
EQVKVFTTRP DTLFGATFMS LAPEHPMAKT LVTAEQKTAV DEFVAKVERQ DKIERTSGDL
EKLGVFTGSY CINPLNGNKI PVFLANFVLM DYGTGAVMAV PAHDQRDFEF ARKYELPITV
VIQPEGDELI AEQMEEAYVG PGSLVNSGRF DGVDNESAKE KIAAYLDERS EGRKTVNFRL
RDWGVSRQRY WGTPIPVIYC DSCGAVPVPE KDLPVILPDD VELTGEGGSP LARHEEFLKV
DCPKCGKAAR RESDTFDTFV ESSWYFARYA CPDYTDGPLD KEAANYWMPV DQYIGGIEHA
VMHLLYARFF TKVLRDLGMI DVDEPFTNLL TQGMVCMETQ RCAEHGWLYP EQIKDGKCTL
CGKTAELGRT EKMSKSKKNV IDPNALIDQY GADTARLFSL FAAPPEKDLE WNEQGVEGCS
RFLGRVWRAV LDNMELIGSA EIPSDASGSA ADLRRKTHQT IKKVTEDVDG RFHFNTAIAA
VMELVNAIYA FKDGEQNPGV LREALEAVVR LLNPFVPHAC EELWEVLGHN ESIEKAGWPK
WDDAALVADE ITLVVQVNGK VRGKVEIAVD ADKETAEKAA LAESNVQRFV EGKQVRKIIV
VPGRLINIVV S
//
