ID A0A098R3P3_9SPIO Unreviewed; 551 AA.
AC A0A098R3P3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 ORFNames=DC28_04665 {ECO:0000313|EMBL:KGE73302.1};
OS Spirochaeta lutea.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73302.1, ECO:0000313|Proteomes:UP000029692};
RN [1] {ECO:0000313|EMBL:KGE73302.1, ECO:0000313|Proteomes:UP000029692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC230 {ECO:0000313|EMBL:KGE73302.1,
RC ECO:0000313|Proteomes:UP000029692};
RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT "De novo Genome Sequence of Spirocheata sp.";
RL Submitted (MAY-2014) 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: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 -!- 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:KGE73302.1}.
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DR EMBL; JNUP01000040; KGE73302.1; -; Genomic_DNA.
DR RefSeq; WP_037546421.1; NZ_JNUP01000040.1.
DR AlphaFoldDB; A0A098R3P3; -.
DR STRING; 1480694.DC28_04665; -.
DR eggNOG; COG1384; Bacteria.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000029692; 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:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00674; LysRS_core_class_I; 1.
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:UP000029692}.
FT MOTIF 43..51
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 293..297
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 551 AA; 62701 MW; 810102EF8C5936F6 CRC64;
MSTNQSTHWA DINADKILRT RQASSDDRGN QNHQFVCASG ITPSGTVHIG NFREIMSVDL
VVRALADKGA KVRFIYSWDD YDVFRKVPKN MPNPEELEKY LRWPITMVPD PHGKEESYAR
ANERAVEELL VQVGIQPEYI YQASKYRAGD YAQGIRTALE HRDTIRGILD QYRSQPLPED
WWPVSVFSSF THKDTTTVLA WDGEWGLTYR CDETGKEETL DLRSTSNAKL PWRVDWPMRW
AYEGVDFEPA GKDHHSEGGS FDTSKQICKA VYGVDAPVTF QYDFISIKGR GGKISSSSGE
VISLDDVLEV YTPQVTRYLF AGTRPNTEFA ISFDLDVIKI YEDYDRCERI YFGIDQVNEK
KAAKERRIYE LSQVHGPMES QPFQLPFRHL CNLLLIMNGD IDRAIRAFEE VPALESQGAL
GEQWWAQARQ RAACAWRWLH SFAPEDFVFT LREPQDGPAD LSAWEGAPPE AISRAALKAL
ADLVSRGISQ YSDKELQDAM YGLSREAGIE PKDFFTVMYQ VLIGRQKGPR LAGFLKTLGQ
ERVAAILALY L
//
