SYL_SHESA
ID SYL_SHESA Reviewed; 859 AA.
AC A0KTW7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Shewana3_1001;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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}.
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DR EMBL; CP000469; ABK47236.1; -; Genomic_DNA.
DR RefSeq; WP_011716120.1; NC_008577.1.
DR AlphaFoldDB; A0KTW7; -.
DR SMR; A0KTW7; -.
DR STRING; 94122.Shewana3_1001; -.
DR EnsemblBacteria; ABK47236; ABK47236; Shewana3_1001.
DR KEGG; shn:Shewana3_1001; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002589; 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 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_1000009426"
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; 96790 MW; 29C0E56CA7FA8B4A 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 AAQTNPELAQ FIEECKNSTT SEADLATMEK
RGVATGLYAI HPITGKQVPI 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