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Database: UniProt
Entry: A0A2N0ERG4_9FLAO
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ID   A0A2N0ERG4_9FLAO        Unreviewed;       941 AA.
AC   A0A2N0ERG4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=ATE92_0809 {ECO:0000313|EMBL:PKA82673.1};
OS   Ulvibacter sp. MAR_2010_11.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacter.
OX   NCBI_TaxID=1250229 {ECO:0000313|EMBL:PKA82673.1, ECO:0000313|Proteomes:UP000232889};
RN   [1] {ECO:0000313|EMBL:PKA82673.1, ECO:0000313|Proteomes:UP000232889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2010_11 {ECO:0000313|EMBL:PKA82673.1,
RC   ECO:0000313|Proteomes:UP000232889};
RA   Teeling H.;
RT   "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT   Genomic & Taxonomic Observatory).";
RL   Submitted (NOV-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   -!- 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:PKA82673.1}.
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DR   EMBL; PHTY01000001; PKA82673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0ERG4; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000232889; 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; 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}.
FT   DOMAIN          39..177
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          279..459
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          792..903
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           714..718
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         717
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   941 AA;  107909 MW;  4A10E9484FF446D1 CRC64;
     MSKYHFNDIE AKWQKYWAEN QTFNAENKSD KPKYYVLDMF PYPSGAGLHV GHPLGYIASD
     IYARYKRHKG FNVLHPQGYD SFGLPAEQYA IQTGQHPRKT TDENIARYRE QLDKIGFSFD
     WSREVRTSDP HYYKWTQWIF MQLFESWYCK KYEKAMPISE LVKLFSEEGN ARINAECETN
     TTEFSADEWN SFSEERKEKI LLKYRLTYLA ETEVNWCPQL GTVLANDEIV NGVSERGGFP
     VIRKRMMQWS MRITAYAQRL LDGLDTIDWP QPLKDSQTNW IGRSKGASVH FKLKDHDGSI
     EVFTTRPDTI YGVSFMTLAP EHELVDRITT MEQRFEVSKY IEATAKRSER ERMADVKTIS
     GVFTGAYAIH PFSGEVIPIW IGDYVLAGYG TGAVMSVPCG DQRDYDFAKH FNIPIPNIFE
     GVDISEEAFS DKDTSIIANS DFLNGLNYAE ATQKAIEALE AKNAGEGKIN YRLRDAVFSR
     QRYWGEPFPV YYKNGLPKLI DAKHLPLTLP EVEKYLPTED GEPPLGRADV WAWDAKQFKV
     VSNQLIDNET VFPLELNTMP GWAGSSCYMF RYMDPHNTKA LASKAAMEYW ENVDLYVGGS
     EHATGHLLYS RFWVKFLFDR GFLPVEEPFK KLINQGMILG ESAFVHRLEG ENVFVSKSKI
     SGRATQPIHA DVSFVNLQNE LDINAFKNWR EDYKDAEFIT EDDGTFKVSR EVEKMSKSKY
     NVVNPDSICK DYGADTLRMY EMFLGPLEQA KPWNTAGITG VHSFLKKLWK LYHTGPDESF
     GFSYEAPTKN NLKTLHKTIK KVQEDIENFS FNTSVSTFMI AVNELTTQKC TTKDILEPLA
     ILISPYAPHI AEELWEKLGH RESISTAAFP KFDASHLVEN TKEYPVSFNG KMRFTLELPL
     DLSKDDIEAA VMSHEKTAHY LEGRTPKKII IVPGKIVNIV G
//
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