ID A0A1Q6NDD4_9CLOT Unreviewed; 489 AA. AC A0A1Q6NDD4; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 20-DEC-2017, entry version 5. 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 RT communities."; RL Nat. Biotechnol. 34:1256-1263(2016). CC -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate CC + L-lysyl-tRNA(Lys). {ECO:0000256|HAMAP-Rule:MF_00252, CC ECO:0000256|RuleBase:RU000336, ECO:0000256|SAAS:SAAS00675040}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00252, ECO:0000256|RuleBase:RU000336}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00252, 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 CC family. {ECO:0000256|HAMAP-Rule:MF_00252, CC ECO:0000256|SAAS:SAAS00675054}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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:0016874; F:ligase activity; IEA:UniProtKB-KW. 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 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; 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|HAMAP-Rule:MF_00252, KW ECO:0000256|SAAS:SAAS00675073}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|SAAS:SAAS00675071}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000187212}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|SAAS:SAAS00675072, ECO:0000313|EMBL:OLA03660.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|RuleBase:RU000336}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|RuleBase:RU000336}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|SAAS:SAAS00675044}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|SAAS:SAAS00684990}. FT DOMAIN 171 482 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE: FT PS50862}. FT COILED 2 22 {ECO:0000256|SAM:Coils}. FT METAL 398 398 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00252}. FT METAL 405 405 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00252}. FT METAL 405 405 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT 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 //