ID A0A0Q9ZGE6_9FLAO Unreviewed; 938 AA.
AC A0A0Q9ZGE6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=APR42_09485 {ECO:0000313|EMBL:KRG27969.1};
OS Salegentibacter mishustinae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salegentibacter.
OX NCBI_TaxID=270918 {ECO:0000313|EMBL:KRG27969.1, ECO:0000313|Proteomes:UP000051643};
RN [1] {ECO:0000313|EMBL:KRG27969.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12263 {ECO:0000313|EMBL:KRG27969.1};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Salegentibacter mishustinae KCTC 12263.";
RL Submitted (OCT-2015) 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: 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:KRG27969.1}.
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; LKTP01000034; KRG27969.1; -; Genomic_DNA.
DR RefSeq; WP_057482641.1; NZ_QKZW01000004.1.
DR AlphaFoldDB; A0A0Q9ZGE6; -.
DR STRING; 270918.APR42_09485; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000051643; 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 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:UP000051643}.
FT DOMAIN 38..152
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 277..458
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 707..739
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 789..902
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 713..717
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 716
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 938 AA; 107409 MW; EAB49D3A34F58590 CRC64;
MSYNFNEIEA KWQKYWAENQ TFRASNSSDK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
YARYKRHTGH NVLHPQGYDS FGLPAEQYAI QTGQHPALTT AKNIKRYREQ LDKIGFSFDW
SREVRTSDPE YYKWTQWIFI QLFESWYDME AEKSRDISEL EEIFSAEGNS RLNAACDDEV
EEFSADAWNA FSSEEKQQIL LKYRLTYLAE TEVNWCPQLG TVLANDEIVN GVSERGGYPV
VRKKMTQWSM RISAFSERLL QGLDQLDWTE SLKESQRNWI GKSVGAHVDF NVQDSDDKIG
VFTTRPDTIF GVTFMTLAPE HELVKKITTP QQKEEIEAYV AASAKRSERE RMADVKSITG
VFTGAYAEHP FTGESIPIWI GDYVLAGYGT GAVMAVPCGD QRDYDFARHF DIPIKNIFEN
ADISEAAFSG KEGTVIANSD FLSGLEYKEA LQKVILELEK TGHGYGKTNY RLRDAVFSRQ
RYWGEPFPVY YVKGMPQMID AQHLPLHLPE VEKYLPTESG EPPLGNATDW AWDTKSNEVV
SNEKIDDETI FPLELNTMPG WAGSSWYLFR YMDSGNDKEF VSKEAQNYWE NVDLYIGGSE
HATGHLLYSR FWTKFLHDRG YLSVEEPFKK LINQGMILGQ SAFVYRLEGE NVFVSKNLIG
ENNVQPIHAD VSLVNHSDEL DIEGFKKWRP EFKDAKFLTE KEGAYIVGRE VEKMSKSKYN
VVNPDDICED YGADTLRMYE MFLGPLEQAK PWNTAGITGV HNFLKKLWKL YHNGEQFEVS
EEKASADSLK SLHKTIKKVT EDIEEFSFNT SVSTFMICVN ELSAQKCNSR EVLEPLVILI
APYAPHIAEE LWSKLGHSES VVTEEYPVFE EKFLVESTKN YPVSFNGKMR FTMELPLDMP
KDEIEKTVMA DERTQKQLDG RTPKKVIVVP GKIVNIVG
//