ID A0A1H8WTP8_9EURY Unreviewed; 562 AA.
AC A0A1H8WTP8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=SAMN04487948_14118 {ECO:0000313|EMBL:SEP30853.1};
OS Halogranum amylolyticum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=660520 {ECO:0000313|EMBL:SEP30853.1, ECO:0000313|Proteomes:UP000199126};
RN [1] {ECO:0000313|EMBL:SEP30853.1, ECO:0000313|Proteomes:UP000199126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10121 {ECO:0000313|EMBL:SEP30853.1,
RC ECO:0000313|Proteomes:UP000199126};
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; FODV01000041; SEP30853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8WTP8; -.
DR OrthoDB; 6838at2157; -.
DR Proteomes; UP000199126; 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; 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}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 61..69
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 326..330
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 63426 MW; A2BD969C4EF77CF8 CRC64;
MSADDTPQPR DTNRAQTTGA DTTDPSEGGD DHRVFWADEM ADRIEARDPE EPVVVKGGVS
PSGIPHLGHF NEILRGFFVA EVLRDRGYEV RQVFTSDDKD ALRKVPRQLA DADWNIVGLG
DVDAGALGRN LGKPYTDIPD PFGDHDSYGD HFADLLHQSA ELLDVPVEML SNTALYADGT
FDEVVRYVLE HREEAREILA NYQDKIDEDY VPFQAQCSEC GVLTTNITGV DLEAETVDYV
CEGLEAGGQQ IDGCGHDGTA TFREGKLPWR FEWPGQWQVL GVDFEPFGKD HAEGSWPSGK
DIAENFLHIR APVPMTYEWF TLNGEALSSS SGNVVTVHEV LELLEPEVLR YFFVRNPKKA
KDFDISRLDQ LVDEFDRFEA IHFGEVDDES LKPLADRAYP FTVDDVREDR VRLPYTFAAV
LGMTDDEDLR EQMARNEGHI TDDTPEWAIE EAMKRVEKAR NWAERLDNEY NYRLQVDLPR
TDFDDEVAAA LDELADFVAA GHSGEEIQGE IYETAKRNDV ATGDFFQAGY RLFFDATQGP
RLGTFLGELD SEFVVKRLRR EE
//
