ID A0A2N5WXU8_9GAMM Unreviewed; 819 AA.
AC A0A2N5WXU8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=C0039_18770 {ECO:0000313|EMBL:PLW67062.1};
OS Pseudohalioglobus lutimaris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohalioglobus.
OX NCBI_TaxID=1737061 {ECO:0000313|EMBL:PLW67062.1, ECO:0000313|Proteomes:UP000235005};
RN [1] {ECO:0000313|EMBL:PLW67062.1, ECO:0000313|Proteomes:UP000235005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF004 {ECO:0000313|EMBL:PLW67062.1,
RC ECO:0000313|Proteomes:UP000235005};
RA Du Z.-J., Shi M.-J.;
RT "The draft genome sequence of Halioglobus lutimaris HF004.";
RL Submitted (JAN-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLW67062.1}.
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DR EMBL; PKUS01000039; PLW67062.1; -; Genomic_DNA.
DR RefSeq; WP_075998935.1; NZ_PKUS01000039.1.
DR AlphaFoldDB; A0A2N5WXU8; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000235005; 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; 3.10.20.590; -; 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:UP000235005}.
FT DOMAIN 40..181
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..407
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 420..618
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 662..780
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 579..583
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 819 AA; 91936 MW; 81AEDEC21F985DA0 CRC64;
MDQQYDPKTL EQNAQAHWLA NNSFAVQQDD SREKFYCLAM FPYPSGKLHM GHVRNYTIAD
VIARYQRMQG KNVLQPMGWD AFGLPAENAA IKNNVPPATW TAQNIDYMRK QLRELGFAYD
WDREIATCDP DYYRWEQWFF TRLFEKGLAY KKKAEVNWCE TDQTVLANEQ VVDGCCWRCD
NPVERREIDQ WFIKITDYAE QLLTDLDGLD QWPEQVRTMQ RNWIGRSEGV ELDFDYNGQP
LSVYTTRPDT LMGATYLAVA PQHPLAQAAA ENIPELAAFV EAQSNIKVAE ADMATMEKLG
MATGLAATHP LTGEQVPIWV ANFVLMSYGS GAVMSVPAHD ERDHAFATKY GLPIVQVVAR
TDDNHVYSSH TWQDWYADKT ETVTINSGEF DGLDFEAAFN AIADRLESQG KGMRKVNYRL
RDWGVSRQRY WGAPIPIINC DSCGAVPVPA EDLPVVLPTD VAFDGVGSPI KQMPEFYQTS
CPTCGGEAVR ETDTFDTFME SSWYYARYGC ANNNRAMLDG EADYWTPVDQ YVGGIEHAIL
HLLYSRFYHK LMRDEGLINS DEPFTRLLTQ GMVLKDGAKM SKSKGNTVDP QALIDRYGAD
TVRLFSMFAA PPEQSLEWSD SGVEGANRFL RRLWKLVSEH LAAAPAPALD ADALNEQQKN
TRRKTHETIA KVGDDYGRRQ TFNTAIAAVM ELCNELGKLD ASEQSRAVMA EALRAVVLML
NPIVPHACHA LWPALGGEGD VLNAAWPCVD ERALARDSIE MVVQVNGKVR AKMQVDATAD
KATAEAAALE QENVRRFLEG VTVRKVIVVP GKLVNIVAN
//
