ID A0A1I2JVS0_9BACT Unreviewed; 927 AA.
AC A0A1I2JVS0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04488541_10676 {ECO:0000313|EMBL:SFF58148.1};
OS Thermoflexibacter ruber.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Thermoflexibacteraceae;
OC Thermoflexibacter.
OX NCBI_TaxID=1003 {ECO:0000313|EMBL:SFF58148.1, ECO:0000313|Proteomes:UP000199513};
RN [1] {ECO:0000313|EMBL:SFF58148.1, ECO:0000313|Proteomes:UP000199513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GEY, DSM 9560 {ECO:0000313|Proteomes:UP000199513};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FONY01000067; SFF58148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2JVS0; -.
DR STRING; 1003.SAMN04488541_10676; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000199513; 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; 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; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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:UP000199513}.
FT DOMAIN 11..144
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 283..462
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 700..727
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 778..892
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT BINDING 704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 927 AA; 106156 MW; 9283B6439DA7DA50 CRC64;
MEYNHKDIEA KWQKYWEENQ IYKVENDTSK PKFYALDMFP YPSGAGLHVG HPLGYIASDI
VARYKKLKGF NVLHPMGFDA FGLPAEQYAI ETGQHPAITT AKNIDTYKKQ LRKIGFNYDW
SREVQTCDPA YYKWTQWIFA QLFNAWYDYS DPANEGLGKA KHIDLLIQTF EKEGNANINA
ACDEDTPVFS AQEWQNFSEK EKSDILLKYR LTYLSEAIVN WCPALGTVLA NDEVKDGFSE
RGGYPVERKK MKQWMMRITA YAERLLAGLE KIDWSESLKE SQRNWIGKSY GAELDFKVEG
KDITLTVFTT RIDTTFGVTF VSIAPEHELI PILTSPEHKA AVEEYVSKAK NRSERERMAD
VKTVSGVFTG SYVINPFSGE KVELWVADYV LAGYGTGVVM AVPSSDDRDF RFAKHFNLPI
IYVIEGTETM ENPTEKKKGK MINSGFLNGL ESDEAIQVAI KFAEEKGIGK GKINYRIRDA
VFSRQRYWGE PVPVYFKDGI PYLLDSSELP LVLPEIDEYK PTETGEPPLG RAKDWKYQNQ
YSYELSTMPG WAGSSWYFLR YMDAQNEKEF VSKEAVNYWG AVDLYIGGTE HAVGHLLYSR
FWNLALYDLG FIGHDEPFQK LINQGMIQGE SALAYRINGT NKFVSKGLKD QYEVAELHVD
VNIVENDVLD IEAFKKWRPD LAEAEFILED GKYICGSAVE KMSKRLYNVV NPDDIVEKYG
ADTLRLYEMF LGPLEQSKPW STKGIDGTYK FLRKLWKLFF DEKGNFNISD AEPTKEELKI
LHKTIKKVAE DIERYSFNTS VPAFMICVNE LTDLKCNKAK VLEPLLIILS PYAPHITEEL
WAKMGHVTSI TRATFPEFNE EYLKESAFEY PISVNGKVRT KIEFPVDKPA KEIETEVLAS
EAIKKWTDGK PIKKVIVVQN KIVNVVV
//
