ID A0A1H3E0B6_9EURY Unreviewed; 553 AA.
AC A0A1H3E0B6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216564_101229 {ECO:0000313|EMBL:SDX72087.1};
OS Halopenitus persicus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1048396 {ECO:0000313|EMBL:SDX72087.1, ECO:0000313|Proteomes:UP000199079};
RN [1] {ECO:0000313|EMBL:SDX72087.1, ECO:0000313|Proteomes:UP000199079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC30,IBRC 10041,KCTC 4046 {ECO:0000313|Proteomes:UP000199079};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNPC01000001; SDX72087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3E0B6; -.
DR OrthoDB; 6838at2157; -.
DR Proteomes; UP000199079; 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; 1.10.10.770; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
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; 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.
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}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 317..321
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 553 AA; 61612 MW; D5D987F63CA7F262 CRC64;
MAEPDADADA RGNSADASSE ETHHAFWADA VADEILERDP AEPIVIKGGV SPSGVAHLGN
FNEIMRGYFV AEVLRERGHE VRQVFTSDDR DPLRKVPRKL ANADGEIVGL GEVDAGALGR
NLGKPYTDIP DPFGEADSYA AHFASLLAAD ADRLGIPVEM VSNTELYADG TFDPVVRTVL
ENAGTAREVL AAYQDKVDEE YVPFNPICEE CGKVTETVTA VDLEAETVEY VCTDMEAGDS
TIEGCGHAGT ATFREGKLPW RFEWPGQWDV LGVDFEPFGK DHAEGSWPSG VDIAETVLGI
DPPVPMVYEW FTLNGKALSS SAGNIVTVPE ILALLEPEVL RYFFALEPKK ARDLDLERLD
QLVDRFDRFE RAYFGAVDDA DLTAVAERAY PFLVEEVREE RVRLPYTFAA VLGMVEDEAF
REQLARDEGH FDDDTPEWAI EDALDRVERA RRWAERMDNE YNYRLQTELP DVSVDEDTAA
ALDDLADFVA EGHDGEAIQE RMYETARDHG LAVADFFEAG YRLFFDETQG PRLGEFLGEL
EREFVVNRLR REA
//
