ID   SYK_BORAF               Reviewed;         521 AA.
AC   Q937W6;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; Synonyms=lysK;
OS   Borreliella afzelii (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=29518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DK26;
RA   Ibba M.;
RT   "Differentiation of Borrelia burgdorferi sensu lato strains using class I
RT   lysyl-tRNA synthetase encoding genes.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR   EMBL; AJ416851; CAC95160.1; -; Genomic_DNA.
DR   RefSeq; WP_004789499.1; NZ_CP018262.1.
DR   AlphaFoldDB; Q937W6; -.
DR   SMR; Q937W6; -.
DR   PRIDE; Q937W6; -.
DR   OMA; DWPMRWA; -.
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; 3.40.50.620; -; 2.
DR   Gene3D; 6.10.20.10; -; 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   PANTHER; PTHR37940; PTHR37940; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00467; lysS_arch; 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.
FT   CHAIN           1..521
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152735"
FT   MOTIF           32..40
FT                   /note="'HIGH' region"
FT   MOTIF           280..284
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   521 AA;  61045 MW;  53DCA9BD31685E32 CRC64;
     MKTAHWADFY AEKIKKDKGP KNLYTVASGI TPSGTVHIGN FREVISVDLV ARALKDSGSK
     VRFIYSWDNY DVFRKVPKNM PEQELLTTYL RQAITRVPDT RSHKTSYARA NEIEFEKYLP
     IVGINPEFID QSKQYTNGVY ASQIKFALNH KKELSNALNE YRTSKLEENW YPISIFCTKC
     NRDTTTVNNY DNHYSVEYSC ECGNQESLDI RTTWAIKLPW RIDWPMRWKY EEVDFEPAGK
     DHHSSGGSFD TSKNIVKIFQ GSPPVTFQYD FISIKGRGGK ISSSSGDVIS LKDVLEVYTP
     EVTRFLFAST RPNTEFSISF DLDVIKIYED YDRFERIYYG VEDIKEEKKR AFKRIYELSQ
     PYMPSKRIPY QIGFRHLSVI CQIFENNINK ILNYLKNVQE DQKDKLINKI KCAINWIRDF
     APEDFKFSLR SKFDSIEILK ENSKKAINEL LNFLKKNFEV ATEQDIQNEI YKISRENNIE
     PALFFKQIYK ILIDKEKGPK LAGFIKIIGI ERFEKIVSRY I