ID A0A3D8LG25_9BACT Unreviewed; 923 AA.
AC A0A3D8LG25;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=DXT99_03800 {ECO:0000313|EMBL:RDV16338.1};
OS Pontibacter diazotrophicus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1400979 {ECO:0000313|EMBL:RDV16338.1, ECO:0000313|Proteomes:UP000256708};
RN [1] {ECO:0000313|Proteomes:UP000256708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4X {ECO:0000313|Proteomes:UP000256708};
RA Liu Z.-W., Du Z.-J.;
RL Submitted (AUG-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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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:RDV16338.1}.
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DR EMBL; QRGR01000004; RDV16338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8LG25; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000256708; 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; 3.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; 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 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}; Cytoplasm {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:UP000256708}.
FT DOMAIN 13..145
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 278..459
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 774..887
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 697..701
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 923 AA; 106785 MW; D8C90D3D73A85907 CRC64;
MSEYNFNQIE KKWQRYWEEN HTFKATAKSD KPKYYAMDMF PYPSGSGLHV GHPLGYIASD
IVSRYKRLTG HNVLHPMGFD SFGLPAEQYA IQTGQHPAIT TEENITRYVE QLKNLGFSFD
WDLEIRTSDP SYYKWTQWIF MQLFNSYYNI NSDKAEPITE LVKEFEQHGN KNVNAACDED
TPAFSADKWK QMNEQEQSEM LLKYRLTYVA EAVVNWCPAL GTVLANDEVV GGVSERGGYP
VERKLMRQWM MRITAYAERL LQGLENIDWP EPVKEMQRNW IGKSVGAIMS FPLESIDKKI
KVFTTRLDTV YGVTFLVLAP EHELVEQITS EEQRKTVEDY VNVAKNRSER ERMTDVKTVS
GAFTGAYAIN PYNNERIPVY IADYVLAGYG TGAVMAVPSG DQRDWNFAKH FGLPIVQILD
GQKDLDTQAD ATKEGHYVNS EMVNGLTYQE ALPVLVKYLE ENNIGKSKIN FRMRDAVFSR
QRYWGEPVPV YFEDGVPHLL DVSDLPLELP KIDAYLPTET GEPPLGRAVD WKYEDEYPYE
LSTMPGWAGS SWYWYRYMDP KNDEAFADKD IIKYWRDVDL YIGGSEHATG HLLYSRFWNK
FLFDMGLVVE EEPFKKLINQ GMIQGRSNFV YRVKDSNTFV SHGLKDQYDT TALHVDVNIV
DNDMLDLEAF KKWRAEYETA EFILEDGKYI CGVEIEKMSK SKYNVVNPDD IVERQGADTL
RMYEMFLGPL EQFKPWNTNG MDGVNKFLKR YWKLFHDNAG NFNVSDEAPN AEELKSLHKT
IKKVEEDIER FSFNTSVSTF MICVNELTQL KTNKRAILEP LTIILSPYAP HITEELWEKL
GHNESISYAA FPQWEERHLV ESTFEYPVSI NGKMRAKMTF SLDTPREEME KAVVNDEQVA
KFMEGKAPKK IIIVPNKIIN VVV
//
