ID A0A3L7JTY5_9BACI Unreviewed; 522 AA.
AC A0A3L7JTY5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=D9X91_14945 {ECO:0000313|EMBL:RLQ94347.1};
OS Falsibacillus albus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Falsibacillus.
OX NCBI_TaxID=2478915 {ECO:0000313|EMBL:RLQ94347.1, ECO:0000313|Proteomes:UP000276770};
RN [1] {ECO:0000313|EMBL:RLQ94347.1, ECO:0000313|Proteomes:UP000276770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GY 10110 {ECO:0000313|EMBL:RLQ94347.1,
RC ECO:0000313|Proteomes:UP000276770};
RA Shi S.;
RT "Falsibacillus sp. genome draft.";
RL Submitted (OCT-2018) 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:RLQ94347.1}.
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DR EMBL; RCVZ01000010; RLQ94347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L7JTY5; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000276770; 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 Gene3D; 1.10.10.350; -; 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:UP000276770}.
FT MOTIF 29..37
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 280..284
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 522 AA; 60100 MW; 9E258AEAD50F3565 CRC64;
MHWAFKMAGQ LIEEHPNAET FVCASGISPS GTVHIGNFRE VVTSYFVVRA LEMLGKNTRF
IFSWDDFDRL RKVPANIDPA HEQYIGMPYS KIPDPNGCHK SYAAHFETEF ENAVKAFGID
AEFIYQNKMY ESGCYHESIL TALNKRKDIY DITMKFKTGG PCEEDRENYY PVAIYCDACR
KDDTNIIAYN QPAESIHYEC SCGHHSEKAV SDLDLKLNWK IDWPMRWQKE SVMFEPGGRD
HSAQTGSYNV SKEIAKEIFD YKAPAYIAYD FIHIKGSQKK MSSSTGISLT PSDLLNVYSP
ELILFLFAKY QPDSAFHIGL DEDVIRNYTE FERYKRAFLA GTLKDDVIRQ ALELVLGEAS
DREEPSFSQL AGILPLVDFN LHLLQEVLQQ NGEQYTMDQL KEVSERVEFW IKHYRQENVN
VINEAPYQKY FDTLTDKEKA QLHHFADIVR EGAAQSGEDL MREIYDICSA ENQKQKKQEQ
KRLFQIIYQL VLNRNSGPRL PILIRAAGAE KIVELVTFDT TS
//
