ID SYL_PSYIN Reviewed; 859 AA. AC A1SU60; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 108. 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=Ping_1191; OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17664 / CCUG 51855 / 37; RX PubMed=18460197; DOI=10.1186/1471-2164-9-210; RA Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J., RA Land M.L., Thompson L.S.; RT "Genomics of an extreme psychrophile, Psychromonas ingrahamii."; RL BMC Genomics 9:210-210(2008). 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; CP000510; ABM03025.1; -; Genomic_DNA. DR RefSeq; WP_011769588.1; NC_008709.1. DR AlphaFoldDB; A1SU60; -. DR SMR; A1SU60; -. DR STRING; 357804.Ping_1191; -. DR KEGG; pin:Ping_1191; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_6; -. DR OrthoDB; 9810365at2; -. DR Proteomes; UP000000639; 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 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..859 FT /note="Leucine--tRNA ligase" FT /id="PRO_1000009402" 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; 96995 MW; B0636E5861FFDE2E CRC64; MQELYNPKEI EKKFQTNWDE NQSFKATEDP SKEKYYCLSM FPYPSGKLHM GHVRNYTIGD VISRYQRMQG KNVMQPMGWD AFGLPAENAA IKNNTAPAGW TYENIAYMKT QLKQLGFGYD WSRELATCQP EYYRWEQWFF TKLVEKDLVY KKMATVNWDP VDQTVLANEQ VIDGRGWRSG ALVEQKEIPQ WFIKITAYAQ ELLDDLDKLD EWPEQVRTMQ RNWIGRSEGV EMDFKVSGKE ESFSVYTTRP DTVMGVTYVA VAAQHPLALE AAKNNPTLAA FCKKCKNVKL AEAEIATMAK EGVDTGFKAI HPISGLEVPI WTANFVLMGY GSGAVMSVPA HDQRDYEFAK KYDLTIKAVI KPANTDLDIS VEAYTEKGVC FDSGEFDGLD FSAAFDAVET KLVAENKGKR QVNFRLRDWG VSRQRYWGTP IPMLNLEDGS VVPVPENELP VILPEDVQMN GIVSPIKADP DWAKTTYNGQ PATHETDTFD TFMESSWYYA RYCSPQSDDA MLDPEKANYW LPVDQYIGGI EHAILHLLYS RFFHKLLRDF GLVDCDEPYK KLLTQGMVLA DAYYYEDAKG GKVWIAPTDV ETETDEKGKV ISAATKDGQT VIYDGMSKMS KSKNNGVDPQ VMIDKYGADS VRLFMMFAAP ADQTLEWSDS ALEGSLRFLK RLWKIAFDHL ALGAVADLDL KSHTEAQKTL RRELHKTIAK VTDDIGRRQT FNTAIASVME LMNKLTKTAT KTEQDRAILQ EALLAITKLL APITPHICAE LFEVLGQTEE ILNAPWPTVD ESALVEDSKL IVVQVNGKLR AKLTVAADAQ QETVQAIAME NENVSKFTDG KTIRKIIFVP GKLLNIVAN //