ID I0WK44_9FLAO Unreviewed; 945 AA.
AC I0WK44;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
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 ECO:0000313|EMBL:EID76760.1};
GN ORFNames=W5A_02015 {ECO:0000313|EMBL:EID76760.1};
OS Imtechella halotolerans K1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Imtechella.
OX NCBI_TaxID=946077 {ECO:0000313|EMBL:EID76760.1, ECO:0000313|Proteomes:UP000005938};
RN [1] {ECO:0000313|EMBL:EID76760.1, ECO:0000313|Proteomes:UP000005938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1 {ECO:0000313|EMBL:EID76760.1,
RC ECO:0000313|Proteomes:UP000005938};
RX PubMed=22740661; DOI=10.1128/JB.00506-12;
RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.;
RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans
RT K1T.";
RL J. Bacteriol. 194:3731-3731(2012).
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:EID76760.1}.
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DR EMBL; AJJU01000002; EID76760.1; -; Genomic_DNA.
DR RefSeq; WP_008236867.1; NZ_AJJU01000002.1.
DR AlphaFoldDB; I0WK44; -.
DR STRING; 946077.W5A_02015; -.
DR PATRIC; fig|946077.3.peg.412; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000005938; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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-RELATED; 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:UP000005938}.
FT DOMAIN 38..145
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 277..464
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 713..746
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 793..907
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 720..724
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 945 AA; 108719 MW; 1E5F19DA38126992 CRC64;
MRYDHRKIEA DWQAYWAKNK TFKADNAFDK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
YARYKRHQGF NVLHPMGYDS FGLPAEQYAI QTGQHPAITT QTNINRYREQ LDKIGFSFDW
EREVRTSNPE YYKYTQWIFI QLFDSWYDKR EDKAKSIETL IEEFEKNGNS LVQAACDEGT
PAFTAQHWKE YTAEEQQKML LKYRLTYLAE TEVNWCPALG TVLANDEIIN GVSERGGHPV
IRKKMTQWSM RISAYAQRLL DGLDTIDWSE SLKESQRNWI GRSQGAMVVF KVIPKNESRD
SMDSIQVFTT RPDTIFGVSF MTLAPEHELV SKITTNEQRA EVEAYIEATA KRSERDRMSD
VKTISGVFTG AYAEHPFTKQ PIPVWIGDYV LAGYGTGAVM AVPCGDDRDY AFAKHFGIEI
LNIFDQDISK AAFTAKEGFS LVNSDFLNGL DYKEGTRLVI DKLEKLGAGT SKINYRLRDA
VFSRQRYWGE PFPVYYVNGL PRMIEKKYLP VRLPEVEKYL PTEDGQPPLG NATVWAWDTE
THTVVSNEYI NHTTVFPLEL NTMPGWAGSS WYWMRYMDAH NEEDFASEKA LRYWQNVDLY
IGGSEHATGH LLYSRFWNKF LRDRGYINIE EPFKKLINQG MILGMSAFVY RTEDAKKLIS
KNKIGNTKVF PIHVDLSVIN DITNELDIEA FKNHPLYADY KNVEFVLEDG KYIVGREVEK
MSKSKYNVVN PDDICDEYGA DTLRLYEMFL GPLEQAKPWN TAGITGVSGF LKKLWRLYFD
EEGFIVTKEE PSKEMYKSLH KTIKKVTEDI ESFSFNTSVS QFMICVNELS QQKCHHQAIL
EPLAVLVSPY APHIAEALWE ALGHNESISN EPFPVCQESY LIESSKEYPV SFNGKMRFKI
ELPLDMTAED IEKLIVADSR TIEQLQGRTP KKIIVVPGKI INIVG
//