ID A0A0G3WIA2_9BACT Unreviewed; 823 AA.
AC A0A0G3WIA2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:AKL97597.1};
GN ORFNames=Epro_0218 {ECO:0000313|EMBL:AKL97597.1};
OS Endomicrobium proavitum.
OC Bacteria; Elusimicrobiota; Endomicrobiia; Endomicrobiales;
OC Endomicrobiaceae; Endomicrobium.
OX NCBI_TaxID=1408281 {ECO:0000313|EMBL:AKL97597.1, ECO:0000313|Proteomes:UP000035337};
RN [1] {ECO:0000313|EMBL:AKL97597.1, ECO:0000313|Proteomes:UP000035337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rsa215 {ECO:0000313|EMBL:AKL97597.1,
RC ECO:0000313|Proteomes:UP000035337};
RA Zheng H.;
RT "Complete genome sequence of Endomicrobium proavitum.";
RL Submitted (SEP-2014) 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}.
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DR EMBL; CP009498; AKL97597.1; -; Genomic_DNA.
DR RefSeq; WP_052571547.1; NZ_CP009498.1.
DR AlphaFoldDB; A0A0G3WIA2; -.
DR STRING; 1408281.Epro_0218; -.
DR KEGG; epo:Epro_0218; -.
DR PATRIC; fig|1408281.3.peg.222; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000035337; Chromosome.
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; 1.
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; 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; 2.
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:UP000035337}.
FT DOMAIN 39..186
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 220..413
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 568..630
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 665..784
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 588..592
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 823 AA; 93590 MW; 24632D41BF8E1169 CRC64;
MSDYNHGEVE KKWQKKWADD NIFRAVEREG KEKYYCLVML PYPSGNLHMG HVRNYGIGDV
FARFHKMKGK NVIHPIGWDA FGLPAENAAI KNKIHPAKWT KQNIARMREQ LKTLGISYDW
DREIATCDPE YYKWNQWIFI KMWEKGLVFK KKANVNWCPS CNTVLANEQV SEGKCWRCSS
VTERKDLEQW FIKITDYADE LLEGHKELSG WPEQVLSMQK NWIGKSYGAE VDFKVQAGSS
KDERTSKDTK TLKIFTTRPD TLFGATFMVV APEHEIIHEL ENKIKNIGEV AKYIEATEAK
SNIERSQSKE KTGVKLEGVE AVNPVTGKLI PIFTADYVLT GYGTGAIMAV PAHDQRDHDF
AKKHNIPIVE VIKGSEPFDV QEKAYEGEGV LVNSGEFNGV KSTDAFKIVS EWVQKRGFGK
KTINFKLKDW LISRQRYWGT PIPFIHCPKC ATVPVNEKDL PITLPEDVEF TGSGESPLKT
SKSFLNVKCP KCGANAQRET DTMDTFVDSS WYFARYCDAH NDSAPFDGKK LNYWMPVNQY
IGGIEHACMH LIYSRFWYKV LRDLGLARDN EPFTNLLTQG MVTLGGSAMS KSRGNIVSPD
EIVEKYGADT ARLFILFAAP PQKQLDWSSD GVEGCWRFIN RIWRLQDVVN TKSTNAAADK
DKADLLRIMH KTIKKVTGDI EKEFQFNTAI SSVMELVNAL YSYKFHSNDG GVSKEVYKTI
ILLMTPFTPH LCEEIWSQIG GKGCISAAPW PVYDEKMIKE DSVELPVQIN GKIKAKITAA
ADASQEDVEK IINSDEKILQ QLKDKQVVKF IYVKNKIVTI VVK
//
