ID F5YBY1_LEAAZ Unreviewed; 542 AA. AC F5YBY1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAR-2024, entry version 66. DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177}; DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177}; DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177}; DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177}; GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177, GN ECO:0000313|EMBL:AEF80924.1}; GN OrderedLocusNames=TREAZ_1825 {ECO:0000313|EMBL:AEF80924.1}; OS Leadbettera azotonutricia (strain ATCC BAA-888 / DSM 13862 / ZAS-9) OS (Treponema azotonutricium). OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Breznakiellaceae; OC Leadbettera. OX NCBI_TaxID=545695 {ECO:0000313|EMBL:AEF80924.1, ECO:0000313|Proteomes:UP000009222}; RN [1] {ECO:0000313|Proteomes:UP000009222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9 RC {ECO:0000313|Proteomes:UP000009222}; RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A., RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K., RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R., RA Paulsen I.T.; RT "Complete sequence of Treponema azotonutricium strain ZAS-9."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEF80924.1, ECO:0000313|Proteomes:UP000009222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9 RC {ECO:0000313|Proteomes:UP000009222}; RX PubMed=21326336; DOI=10.1038/ismej.2011.3; RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.; RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut RT spirochete species in co-culture."; RL ISME J. 5:1133-1142(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl- CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA- CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CC Evidence={ECO:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP- CC Rule:MF_00177}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00177}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}. 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; CP001841; AEF80924.1; -; Genomic_DNA. DR RefSeq; WP_015710207.1; NC_015577.1. DR AlphaFoldDB; F5YBY1; -. DR STRING; 545695.TREAZ_1825; -. DR KEGG; taz:TREAZ_1825; -. DR eggNOG; COG1384; Bacteria. DR HOGENOM; CLU_025562_1_0_12; -. DR InParanoid; F5YBY1; -. DR OrthoDB; 9803151at2; -. DR Proteomes; UP000009222; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 1.10.10.770; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 1. DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1. DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf. DR InterPro; IPR002904; Lys-tRNA-ligase. DR InterPro; IPR042078; Lys-tRNA-ligase_SC_fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00467; lysS_arch; 1. DR PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1. DR PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1. DR Pfam; PF01921; tRNA-synt_1f; 1. DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00177}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00177}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00177}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00177}; Reference proteome {ECO:0000313|Proteomes:UP000009222}. FT MOTIF 42..50 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177" FT MOTIF 294..298 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177" SQ SEQUENCE 542 AA; 61709 MW; 34935944DCC4AD3C CRC64; MEKKNEASGA QASAHWADET AAKILREKGD KELYTCASGI TPSGTVHIGN FREIISTDLV VRALRDKGKK VRFIYSWDDY DVFRKVPKNM PQQEALNGHL RFPITMVPDP WGRDSSYARH HEVDIETVLP KVGVHPEFLY QAENYRSSKY AEGIRKALEH REALKNILDK FRDEEHKIQG EWWPVSAFCS ACNKDDTEID SWDGEWGVTY HCNSCGHKET ADIRTAKGIK LFWRIDWPMR WEYEKVDFEP AGKDHHSQGG SFDTAKHVCK DVYDWDAPVT FRYDFIGTKG LPGKMSSSSG NVITIEDVLN VYTPEVARYL FAGTRPNTEF TISFDLDVIK IYEDYDKTER IAFKAEPAKD EAVYQKERRI YELSQAAVTA EGKTKMPEIM PFQVPFRHLC NLIQIADGDI DKAIASIANL KPEQIPALKA RAACAKYWID ECAPEEFRFK LREPGETSDL ADNEKAAIKQ LRDEVISKID SFTDDKGCAE AIYKIAEAQG MEGKALFRAA YQALIGKDQG PRLANFLRSI NKDRLLGILK AY //