ID A0A1F1KZK4_9CORY Unreviewed; 950 AA.
AC A0A1F1KZK4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=HMPREF3067_05745 {ECO:0000313|EMBL:OFS21737.1};
OS Corynebacterium sp. HMSC04H06.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581050 {ECO:0000313|EMBL:OFS21737.1, ECO:0000313|Proteomes:UP000177657};
RN [1] {ECO:0000313|EMBL:OFS21737.1, ECO:0000313|Proteomes:UP000177657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC04H06 {ECO:0000313|EMBL:OFS21737.1,
RC ECO:0000313|Proteomes:UP000177657};
RA Ploux O.;
RL Submitted (MAR-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:RU363039}.
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:OFS21737.1}.
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DR EMBL; LWPR01000037; OFS21737.1; -; Genomic_DNA.
DR RefSeq; WP_070768772.1; NZ_KV823424.1.
DR AlphaFoldDB; A0A1F1KZK4; -.
DR STRING; 1581050.HMPREF3067_05745; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000177657; 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; 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; 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:UP000177657}.
FT DOMAIN 63..168
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 291..475
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 798..913
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 950 AA; 107114 MW; CEC1D0B769925216 CRC64;
MTNPSDSTDT TAHRYTPELA NQIEKTWQQY WADNGTFTAP NPVGDLATDG QLPAEKLNVQ
DMFPYPSGAG LHVGHPLGYI ATDTFARYNR MLGKNVLHTL GYDAFGLPAE QYAIQTGTHP
RTTTMTNIDN MRRQLGALGL GHDPRRSVAT TDPEFYKWTQ WIFLQIYNAW FDEEQGKARP
ISELIQELEA NKRTTKDGRY YEDLTAAEKA EAVDEFRLVY LSNSTVNWCP GLGTVLANEE
VTADGKSERG NFPVFRKNLK QWMMRITAYS DRLLDDLELL DWPEKVKSMQ RNWIGRSRGA
DVNFTAEGQE ITVFTTRPDT LFGAEYVVLA PEHELVDHLL SPIPYDDDID ERWTYGHDDP
KEAVEAYRED IAAKSDLERQ ENKDKTGVFL GTYATNPVSG KQVPIFIADY VLTGYGTGAI
MAVPAHDTRD YEFAQTFGLP ITEVVSGGDV STEAWTEDGT LVNSANDAGL DLNGLDKKAA
IARTIAWLEE TGKGAEKIQY KLRDWLFARQ RYWGEPFPIV YDADGHAHAL PESMLPVELP
EVEDYAPVSF DPEDRNSEPQ PPLAKAREWV EVELDLGDGP QTYYRDTNVM PQWAGSSWYQ
LRYVDPTNDE QFCDLENERY WTGPRPEEHG ANDPGGVDLY VGGVEHAVLH LLYSRFWHKV
LYDLGFVSSK EPYRRLFNQG YIQAYAYTDS RGVYVPAAEV EEKDGKFYYN GEEVNQEYGK
MGKSLKNAVA PDDICRDFGA DTLRVYEMSM GPLDTSRPWA TKDVVGAQRF LQRLWRLAVN
EETGELAATD AALTEDDLKA LHRTIAGVRD DYENLRLNTV VAKLIEYVNY LTKAYSNGAP
RQAVEPIAQM VSPVAPHIAE EIWRRFGHAE TITFEPFPAY EDKYLVDDEI EVPVQINGKV
KSRIHVAADA DQDTVLAAAS ADTKIAELIS GKNVVKQIYV PGRMVNLVVK
//
