SYL_SHESR
ID SYL_SHESR Reviewed; 859 AA.
AC Q0HXU4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049};
GN OrderedLocusNames=Shewmr7_1062;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) 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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|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; CP000444; ABI42061.1; -; Genomic_DNA.
DR RefSeq; WP_011625476.1; NC_008322.1.
DR AlphaFoldDB; Q0HXU4; -.
DR SMR; Q0HXU4; -.
DR EnsemblBacteria; ABI42061; ABI42061; Shewmr7_1062.
DR KEGG; shm:Shewmr7_1062; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
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 Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..859
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009428"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 618..622
FT /note="'KMSKS' region"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 859 AA; 96762 MW; 67902C106BAF69FF CRC64;
MQEQYNPSEI EALVQKHWHD NKTFEVTEDA NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARFQRLQG KNVLQPIGWD SFGLPAENAA INNKTAPAPW TYQNIEYMKN QLKLLGFGYD
WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTASVNWCP NDETVLANEQ VQDGCCWRCD
TPVEQKEIPQ WFIKITAYAE ELLNDIDTLD GWPEQVKTMQ RNWIGRSEGV EMTFGVAGSD
KSFDIYTTRP DTLMGVTYVA IAAGHPLAEL AAQSNPELAQ FIEECKNSTT SEADLATMEK
RGVATGLYAI HPISGKQVPI WAANFVLMNY GTGAVMSVPG HDQRDYEFAK KYNLPIEAVI
KPVDGELDIS EAAYTEKGVL FNSGEFDGLD FDGAFNAIAD KLVAEGKGKR QVNYRLRDWG
VSRQRYWGAP IPMVTLADGT VIPTPEDQLP VILPEDVVMD GIQSPIKADK EWAKTQVNGQ
DALRETDTFD TFMESSWYYA RYCSPQADQM LDPTKANYWL PVDQYIGGIE HACMHLLYFR
FFHKLLRDAG LVNSNEPAKQ LLTQGMVLAD AFYYTNDKGA RVWVSPLDVV TTEKDDKGRV
TKAIDKDGNE LVYTGMCKMS KSKNNGIDPQ VMVEKYGADT VRLFMMFASP PELTLEWQES
GVEGAHRFIK RLWKLASDYV AQDNSEALDV SKLTSEQKAL RREVHKTIAK VTDDIGRRQM
FNTAVAAVME LMNHLQKAPQ TTGQDRAIIG EALTAVVRLL YPIIPHVSFT LWNELGNTNS
IEDSQWPVVD ESALVEDSKL IVVQVNGKVR AKITVAADAD QASVEALGMA DEQVIKYLDG
VTVRKVIYVP GKLLSIVAN