ID A0A1Q6NDD4_9CLOT Unreviewed; 489 AA. AC A0A1Q6NDD4; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-APR-2021, entry version 19. DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252}; DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252}; DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252}; DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252}; GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252}; GN ORFNames=BHW11_00015 {ECO:0000313|EMBL:OLA03660.1}; OS Clostridium sp. CAG:62_40_43. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1896990 {ECO:0000313|EMBL:OLA03660.1, ECO:0000313|Proteomes:UP000187212}; RN [1] {ECO:0000313|EMBL:OLA03660.1, ECO:0000313|Proteomes:UP000187212} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAG:62_40_43 {ECO:0000313|EMBL:OLA03660.1}; RX PubMed=27819664; DOI=10.1038/nbt.3704; RA Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.; RT "Measurement of bacterial replication rates in microbial communities."; RL Nat. Biotechnol. 34:1256-1263(2016). 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_00252, ECO:0000256|RuleBase:RU000336}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00252, CC ECO:0000256|RuleBase:RU000336}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252, CC ECO:0000256|RuleBase:RU000336}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OLA03660.1}. 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; MNSA01000001; OLA03660.1; -; Genomic_DNA. DR EnsemblBacteria; OLA03660; OLA03660; BHW11_00015. DR Proteomes; UP000187212; Unassembled WGS sequence. 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00775; LysRS_core; 1. DR CDD; cd04322; LysRS_N; 1. DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1. DR InterPro; IPR004364; Aa-tRNA-synt_II. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR002313; Lys-tRNA-ligase_II. DR InterPro; IPR044136; Lys-tRNA-ligase_II_N. DR InterPro; IPR018149; Lys-tRNA-synth_II_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR00982; TRNASYNTHLYS. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00499; lysS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00252}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00252}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00252}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000313|EMBL:OLA03660.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|RuleBase:RU000336}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00252}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252}. FT DOMAIN 171..482 FT /note="AA_TRNA_LIGASE_II" FT /evidence="ECO:0000259|PROSITE:PS50862" FT COILED 2..22 FT /evidence="ECO:0000256|SAM:Coils" FT METAL 398 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" FT METAL 405 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" FT METAL 405 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" SQ SEQUENCE 489 AA; 56230 MW; 128A35F0B8602A7B CRC64; MAEDINQLLK VRREKLQNLQ EAGKDPFKIT KCDVTHHSME IKNNYDELEG KTVTIAGRMM FKRVMGKASF CNTRDLEGDI QAYVARDNIG EDSYKDFKKY DVGDLLCITG EVFKTKTGEI SIHASNVTLL SKSLQILPEK FHGLTDTDVR YRQRYVDLIM NAEVKDTFIK RSRIISTIRK YLDGEGFMEV ETPMLVANAG GAAARPFETH FNALDEDFKL RISLELYLKR LIVGGMEKVY EIGRVFRNEG LDTRHNPEFT LMELYQAYTD YHGMMDLTEN LYRYVAQEVL GTTKITYNGI EMDLGKPFER LTMVDAVKKY ADVDFNEIST LEEAQAIAKE KGIEFEPHHK KGDILNLFFE EFVEEHLIQP TFIMDHPIEI SPLTKKKPDN PDYVERFEFF MNGWEMANAY SELNDPIDQR ERFKAQEELL ALGDEEANTT DEDFLNALEI GMPPTGGIGF GIDRMCMLLT DSAAIRDVLL FPTMKSQKE //