ID   SYL_PSET1               Reviewed;         862 AA.
AC   Q3IJ93;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=PSHAa1031;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI86109.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3IJ93; -.
DR   SMR; Q3IJ93; -.
DR   STRING; 326442.PSHAa1031; -.
DR   KEGG; pha:PSHAa1031; -.
DR   PATRIC; fig|326442.8.peg.991; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   BioCyc; PHAL326442:PSHA_RS05040-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome I.
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; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; 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; PF00133; tRNA-synt_1; 2.
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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..862
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009400"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   862 AA;  97721 MW;  323B8C27F25615BB CRC64;
     MQEQYNPQKI ESKIQRYWEE NKVFKVTEDE SKEKYYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRFQRLKG KNVMQPMGWD AFGLPAENAA IKNKTAPAKW TYENIDYMRT QLKQLGFGYD
     WDREIATCHP EYYKWEQWFF TKLYEKGLVY KKMSTVNWDP VDQTVLANEQ VIDGRGWRSG
     AVVEQKEIPQ WFIKITDYAQ ELLDDLDKLE DWPEQVKTMQ RNWIGRSEGC DIEFKRTDNN
     ETFSVYTTRP DTFMGVTYVA VAAGHPIAKE AAKNSDSVAL FVEECKNNKV SEADMATMEK
     KGIATGFFAT HPLTGEQVPI WIANFVLMHY GSGAVMAVPA HDQRDFEFAT AYGLDIKQVI
     APVTGSDLEV NLNKEAFTDK GVLVNSGEFD GLDFDAAFNA IADKLEALGV GERKVNFRLR
     DWGVSRQRYW GSPIPMLSDE DGNELAATDD MLPVRLPEDV VMNGVTSPIK ADPNWAKTTM
     NGAPAFHETD TFDTFMESSW YYARYCSPRH DEGMLDPAAA NYWLPVNQYI GGIEHAILHL
     LYSRFFHKLL RDFGLVDSDE PFDRLLCQGM VLAETFYRKD EKGADIWISP SDVNTETDDK
     GRVTKAWHKV DGNPVFSSGM SKMSKSKNNG IDPQHVIAQY GADTVRLFMM FTAPPEQTLE
     WSDAGVEGAH RFLKRVWKYA VDVKTVGFQP LNKTALNNEQ KVLRRDLHKA IAKVSDDVER
     RQTFNTAIAA IMELSNKLLK APLNSKQDVA IANEALEAML IMLAPITPHL SHQLWQELGK
     EGDIVNASWP EVDQSALVED EKLIIIQVNG KLRAKLTVAA DATKEQVEAL AFEQASVTKY
     TDGVTVRKVI YVPGKLLNVV AN
//