ID A0A1N6X2W7_9BACT Unreviewed; 923 AA.
AC A0A1N6X2W7;
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=SAMN05421545_1898 {ECO:0000313|EMBL:SIQ96724.1};
OS Pontibacter lucknowensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1077936 {ECO:0000313|EMBL:SIQ96724.1, ECO:0000313|Proteomes:UP000185924};
RN [1] {ECO:0000313|Proteomes:UP000185924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM9 {ECO:0000313|Proteomes:UP000185924};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FTNM01000002; SIQ96724.1; -; Genomic_DNA.
DR RefSeq; WP_076421889.1; NZ_FTNM01000002.1.
DR AlphaFoldDB; A0A1N6X2W7; -.
DR STRING; 1077936.SAMN05421545_1898; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000185924; 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; IPR001412; aa-tRNA-synth_I_CS.
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; 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:UP000185924}.
FT DOMAIN 39..155
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 278..458
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 774..886
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; 105744 MW; A5722B89F439817D CRC64;
MSEYNFNQIE KKWQRYWEQN QTFKATDNTD KPKYYVLDMF PYPSGAGLHV GHPLGYIASD
IVSRYKRSKG FNVLHPMGFD SFGLPAEQYA IQTGQHPAIT TEQNIARYIE QLKNIGFSYE
WEREVRTSDP NYYKWTQWIF MQLFNSYYDY TSDKAESIDK LIAAFEANGN ADINAACDED
TPAFTAEDWK GMNEQDKAEM LLRYRLTYVA DAVVNWCPAL GTVLANDEVV GGVSERGGYP
VERKKMRQWM MRITAYAERL LQGLDTIDWP EPVKEMQRNW IGKSVGAELD FAIEGGASEK
IKVFTTRIDT IYGATFVVLA PEHELVNEIT TDAQRTEVER YVNVAKNRSE RERMTDVKTV
SGVFTGAYAI NPISEERVPI WIADYVLAGY GTGAVMAVPG HDSRDYAFAK HFNLTIKEVV
AGGNLEEEAY AGKEGKIINS GFLNGLDVKE AINAGIAKAE ELGVGKGRTQ YRMRDAVFSR
QRYWGEPVPV YFKDGIPRLM DENDLPLELP KIDAYLPTET GEPPLGRAVD WKYQDQYEYE
LSTMPGWAGS SWYWYRYMDP QNDQAFADKA KVEYWRNVDL YMGGAEHATG HLLYSRFWNK
FLCDMGLVVE QEPFKKLINQ GMIQGRSNFV YRVKDSNTYV SYSLRKDYDI TQLHVDVNIV
ENDELDLEAF KAWRPENANA EFILEDGKYI CGVEIEKMSK SKYNVVNPDI IVERNGADTL
RMYEMFLGPL EQFKPWNTNG MDGVTKFLKR FWKLFHDNEG NFTVSDAEPT AEELKSLHKT
VKKVEEDIER FSFNTSVSTF MICVNELTAL KTNKRAILEP LTIALAPYAP HIAEELWEKL
GHTQSITFAS FPAWDEKYLV ENTFEYPVSV NGKTRGKIAF ATDTPREEME KAVLTDETVV
KFMEGKTPKK IIIVPNKIIN VVV
//
