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Database: UniProt
Entry: A0A0Q9ZGE6_9FLAO
LinkDB: A0A0Q9ZGE6_9FLAO
Original site: A0A0Q9ZGE6_9FLAO 
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}.
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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
//
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