ID D1PE82_9BACT Unreviewed; 953 AA.
AC D1PE82;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
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:EFB34950.1};
GN ORFNames=PREVCOP_05530 {ECO:0000313|EMBL:EFB34950.1};
OS Segatella copri DSM 18205.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=537011 {ECO:0000313|EMBL:EFB34950.1, ECO:0000313|Proteomes:UP000004477};
RN [1] {ECO:0000313|EMBL:EFB34950.1, ECO:0000313|Proteomes:UP000004477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18205 {ECO:0000313|EMBL:EFB34950.1,
RC ECO:0000313|Proteomes:UP000004477};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) 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 -!- 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:EFB34950.1}.
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DR EMBL; ACBX02000022; EFB34950.1; -; Genomic_DNA.
DR RefSeq; WP_006848223.1; NZ_VZAC01000089.1.
DR AlphaFoldDB; D1PE82; -.
DR STRING; 537011.PREVCOP_05530; -.
DR PaxDb; 537011-PREVCOP_05530; -.
DR GeneID; 69847976; -.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000004477; 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; 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; 1.
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:UP000004477}.
FT DOMAIN 11..144
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 276..460
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 802..915
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 723..727
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 726
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 953 AA; 109371 MW; 4331073562C1881D CRC64;
MEYNFREIEK KWHQKWVENK TYKVTEDENK KKFYVLNMFP YPSGAGLHVG HPLGYIASDI
YARYKRLNGF NVLNPMGYDA YGLPAEQYAI QTGQHPEVTT IANINRYREQ LDKIGFSFDW
VREVRTCDPK YYHWTQWAFQ KMFNSFFCNS CQKAQPIEKL IKRFEEKGSA DLNVAQNEQI
DFTAEEWNSY DDVKKQQILM NYRIAYLGET MVNWCPGLGT VLANDEVVNG VSERGGYPVI
QKKMQQWCLR TSAYSQRLLD GLETIQWSDS IKETQKNWIG RSEGTEVVFS VKDSDVKFTI
FTTRADTMFG VTFMVLAPES EYVQQVTTAE QKEEVEKYLD YVKKRTELDR MANHSVTGVF
SGSYAINPFT GEAIPIWISE YVLAGYGTGA IMAVPAHDSR DYAFAKHFNL PIIPLIEGAD
VSEESFDAKE GIVTNSPVAG KSSMDGFSLN GLTVKEAIAA TKKFVTEKGI GRVKVNYRLR
DAIFSRQRYW GEPFPVYYKD GMPQMVPEEC LPLELPEIET YKPTETGEPP LGRAKKWAWD
AEKKEVVDKS LVDNKTVFPL ELNTMPGFAG SSAYYLRYMD PHNDEALVSK EADEYWQNVD
LYVGGCEHAT GHLIYSRFWN KFLFDLGVSC KEEPFQKLVN QGMIQGRSNF VYRINSNDHD
KAPVFVSLNL KKDYDVTPIH VDVNIVSNDV LDIEAFKAWR PEYQNAEFIL EDGKYICGWA
IEKMSKSMFN VVNPDMIVEK YGADTLRLYE MFLGPVEASK PWDTNGIDGC HRFLKKFWGL
FYENRTDNFL PSADEAAKPE SLKSVHKLIK KVSEDIEKFS YNTSISAFMI AVNELGQQKC
RNKELLTDLV ILIAPFAPHI AEELWAALGE QGSVCDAAWP KYDEQYLKEN DMQLTISFNG
KARFQMTFPV DTPNEEIQKQ VLEDEKSQKY LEGFNVLKVI IVPKKIVNVV LKK
//
