ID   SYL_DESPS               Reviewed;         827 AA.
AC   Q6AJZ7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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}; OrderedLocusNames=DP2600;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG37329.1; -; Genomic_DNA.
DR   RefSeq; WP_011189841.1; NC_006138.1.
DR   AlphaFoldDB; Q6AJZ7; -.
DR   SMR; Q6AJZ7; -.
DR   STRING; 177439.DP2600; -.
DR   EnsemblBacteria; CAG37329; CAG37329; DP2600.
DR   KEGG; dps:DP2600; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000602; 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; -; 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; 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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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; Reference proteome.
FT   CHAIN           1..827
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152010"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           585..589
FT                   /note="'KMSKS' region"
FT   BINDING         588
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   827 AA;  94774 MW;  908B7BC6238F63D6 CRC64;
     MQHPTNARYD FKTIESKWQK NWAENKTYSV TEDEDKEKYY LLEMFPYPSG RIHMGHVRNY
     TIGDVVARYK RMRGFNVLHP MGWDAFGLPA ENAAQKNNTH PSVWTYDNID YMRQQLQQLG
     LSYDWDREMA TCNPKYYRQE QQLFIEMLEK GLIYEKVTTV NWCDTCQTVL ANEQVIEGAC
     WRCDQLVHPR KMNGWFFKIT DYAEELLADL DKLTGWPEKV RTMQRNWIGK STGLSCDFQL
     EDMDDKISIF TTRPDTIYGV TFMSLAPEHP LVEQLIAGTD REQEVRDFVK EVLEDKQRQD
     PTQEPEKKGI FTGKYCTNPF NGDRVPVYVA NFVLIEYGTG AVMAVPAHDQ RDFEFAGKYK
     LPIIPVVVPE GEAVNPADME EALTNHGLLI NSGDFTGMAS QEAQAKIIAY AEEKGFGSPL
     TTYRLRDWGI SRQRYWGAPI PIIHCDSCGI VPVPIDQLPV ELPEDKDKSS VCAPLHQRPD
     FINTTCPKCG QPAKRETDTM DTFVESSWYF ARYTSPRHTE APLDKAKAKY WLAVDQYIGG
     VEHAILHLLY SRFFTKVLRD LGYLEIDEPF IKLLTQGMVI KDGTKMSKSK GNVVDPHDLI
     SEFGADTTRL FSLFAAPPER DLEWSSEGVE GSSRFLNRIY RFITANFEAL TAGEAFPKKL
     SEEDRLLHRK NHQTIKRVTE NIEHNFHFNT AISAVMELVN QLFAQFKNEK SIAAPAVLRA
     SVDSVLLLLS PMVPHFCNEM WMVLGNTEPI ENQAWPEFDI EATKEDLLTI IIQVRGKVRS
     KIQVPVDIEE DEIVALALAD ENCQKFIDGQ PIKKTIVVKK KLVNIVI