ID A0A238XBJ0_9FLAO Unreviewed; 1073 AA.
AC A0A238XBJ0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN04488111_1690 {ECO:0000313|EMBL:SNR55249.1};
OS Lutibacter flavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=691689 {ECO:0000313|EMBL:SNR55249.1, ECO:0000313|Proteomes:UP000198412};
RN [1] {ECO:0000313|Proteomes:UP000198412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27993 {ECO:0000313|Proteomes:UP000198412};
RA Varghese N., Submissions S.;
RL Submitted (JUN-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:RU363035}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; FZNX01000002; SNR55249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238XBJ0; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000198412; 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 Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR Gene3D; 3.40.960.10; VSR Endonuclease; 1.
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; IPR007569; DUF559.
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; IPR011335; Restrct_endonuc-II-like.
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 PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF04480; DUF559; 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; SSF52980; Restriction endonuclease-like; 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..144
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 315..408
FT /note="DUF559"
FT /evidence="ECO:0000259|Pfam:PF04480"
FT DOMAIN 426..593
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 845..874
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 924..1035
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 848..852
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 851
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 1073 AA; 122371 MW; B5BFE022E01104D1 CRC64;
MEYNFREIEA KWQKYWAENQ TFKAENKSSK PKFFVLDMFP YPSGAGLHVG HPLGYIASDI
YARYKRHKGF NVMHPQGYDS FGLPAEQYAI QTGQHPAVTT EANIKTYRKQ LDQIGFSFDW
SREVRTSDPN YYKWTQWIFI QLFNSWYNKI SDKAEDIETL IAIFSSEGNA AVKAACDEDI
EIFTAKDWKG FSEEQQQNIL LKYRLTFLSE TEVNWCPALG TVLANDEIVN GVSERGGHTV
VRKKMMQWSM RITAYAQRLL DGLAKIDWPQ PLKDSQTYWI GRSEGAMVTF KVLSTSTNSD
IRDMKLSFKE FEKLKENRSN PSKVEGLLWD RLKKKKGSSK FRAKYMVGSF LVDFVCFTKN
TIVEFSGKED EKERSKFFES EGFSVVRISP EDILENIDAV VSKIDSALQF PVISKVNENK
SGNEIPVEKD SGMEISVFTT RPDTIFGVSF MTLAPEHELV SKITTAEQKK DVEAYVKATA
KRSELERMAD VKTISGVFTG AYAKHPFSGE KVQIWIGDYV LAGYGTGAVM AVPCGDERDY
AFAKHFGLDI PNIFEGVDIS EEACSDKEGV KIANSDFLNG LTYKRAMKTI IYEIEKRGIG
FGKINYRLRD AVFSRQRYWG EPFPVYYKNG LPQMIDKQYL PIVLPEVEKY LPTEDGKPPL
GNAAVWSWDT SKNKVVSNDL IDNVTIFPLE LNTMPGWAGS SSYFNRYMDP ENTEEFVSKE
AVEYWQDVDL YIGGSEHATG HLLYSRFWQK FLFDKGIVPV DEYAKKLINQ GMITGTSAFV
YRVEGENKFV SKGLIEGLKV QPIHSDVSFV NGSDELDVEA FKNWREEYKD AEFVLEDGKY
ICGREVEKMS KSKYNVVNPD TICEKYGADS LRLFEMFLGP LEQSKPWKTS GISGVYSFLK
KLWKLYVVNG EFSVSDEEPT ADELKTLHKT IKKVEYDIAN FSFNTSVSNF MIAVNELTAL
ECNKRAILEP LAIIIEPYAP HIAEELWNKL GHKTSVSTEE FPIFEPKYLV ESSKEYPVSF
NGKMRFKIEL SLDLGVKEIE EIVMAHEKTQ AQLQGRTPKK VIIVPGKIIN IVG
//
