ID A0A1M7AFT5_9STAP Unreviewed; 804 AA.
AC A0A1M7AFT5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=SAMN02745189_00139 {ECO:0000313|EMBL:SHL41524.1};
OS Salinicoccus alkaliphilus DSM 16010.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX NCBI_TaxID=1123231 {ECO:0000313|EMBL:SHL41524.1, ECO:0000313|Proteomes:UP000184206};
RN [1] {ECO:0000313|EMBL:SHL41524.1, ECO:0000313|Proteomes:UP000184206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16010 {ECO:0000313|EMBL:SHL41524.1,
RC ECO:0000313|Proteomes:UP000184206};
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:RU363039}.
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; FRCF01000002; SHL41524.1; -; Genomic_DNA.
DR RefSeq; WP_072707332.1; NZ_FRCF01000002.1.
DR AlphaFoldDB; A0A1M7AFT5; -.
DR STRING; 1123231.SAMN02745189_00139; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000184206; 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; 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.
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:UP000184206}.
FT DOMAIN 39..170
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..395
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 411..603
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 654..766
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 575..579
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 804 AA; 92330 MW; FB42E50CA03A9265 CRC64;
MAYNHREIEK KWQEYWESNQ TFKTEEEYDK KKFYALDMFP YPSGSGLHVG HPEGYTATDI
ISRMKRMQGY NVLHPMGWDA FGLPAEQYAI DTGNDIREFN EQNINTFRRQ IKELGFSYDW
DREINTTDPD YFKWTQWIFI QLYNKGLAYI DEVPVNWCEA LGTVLANEEV IDGLSERGGH
PVVRKPMRQW MLKITEYADR LLEDLEELDW PESLKDMQRH WIGKSEGANI DFKIEGKDPH
FTAFTTRPDT IYGATYAVFA PEHKLVDEIT TDEQREAVKA YQDKAAMKSE LERTDLAKEK
TGAFTGAYAI NPFNGEKMPI WISDYVLASY GTGAIMAVPA HDQRDYEFAK AFGLPITGVI
EGGNIEEEAY VGDGPHVNSG ELDGLNTEDA IEKSLEIMVD KGYGRKETTY KLRDWLFSRQ
RYWGEPIPVI HWEDGTMSTV PEDELPLELP VMEQIKPSGT GESPLANNED WIQVVREDGV
KGRRETNTMP QWAGSCWYYL RFIDPHNDEA LADPEKLKHW LPVDLYIGGA EHAVLHLLYA
RFWHKVLYDV GVVHTKEPFQ KLFNQGMILG EGNEKMSKSK GNVINPDDIV YSHGADTLRL
YEMFMGPLDA SVSWSTTGLD GSRRFLDRVW RLVINEETGE LNEKIVDNET PELEKVYHET
VKKVTEDYAS LDFNTAISQM MVFVNECYKS EEVSKAYIEN FAKMLSAIAP HIGEELWGRL
GNPDTLAYAE WPEYDESKLV EDEVEIVIQV NGKVKEKRHV PADASKEDLE RIAIESNKIQ
SELQDKTIRK VIVVPGKLVN IVAN
//
