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
//