ID A0A1F5CRL1_9ARCH Unreviewed; 534 AA.
AC A0A1F5CRL1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=A3K79_03900 {ECO:0000313|EMBL:OGD45496.1};
OS Candidatus Bathyarchaeota archaeon RBG_13_46_16b.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1797378 {ECO:0000313|EMBL:OGD45496.1, ECO:0000313|Proteomes:UP000176481};
RN [1] {ECO:0000313|EMBL:OGD45496.1, ECO:0000313|Proteomes:UP000176481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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: 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:OGD45496.1}.
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DR EMBL; MEZE01000056; OGD45496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5CRL1; -.
DR Proteomes; UP000176481; 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; 2.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
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; 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; PF19269; Anticodon_2; 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 DOMAIN 450..531
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 41..49
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 296..300
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 534 AA; 59633 MW; 1B79CFCC92D5D974 CRC64;
MSEKTIGRGT WYDKMAAKII ERERKIGRSL GLVRTEMGLG ASGFPHIGSL GDAVRSYAVT
LALREQGYCS ELVAYCDDKD GLRKVPAGLP SSLEKYLGFP VTSIPDPYGC HESYGGHMSS
LLLDALDKCG IEYCYMSAKE AYDSGVLNEE TRTLLLNAKK VGEIVKEEVG QERYTEVLPY
FAVCGSCGRL YTTKASKFLP DEGKVLYACE GMEIKGKWIE GCGFKGEADV TKGEGKLTWK
GEFAARWKAL DIRFEAFGKD IADSVRINDR ICREILCHEP PAHAKYEMFL DKSGRKISKS
TGNVFTPQVW FRYGSPQSLL LLMLKRFVGT RTLDVSDIPS YMNELDCLED VYFGRKLAKD
SRELTKIKGL YEYVWSLEPP KKTTVHVPYN LLTFLAKMAP SGNELVFIAE KLQGYGYLSK
DQMPDEDLRK RVGFASNWIK DFEEIKETTV SLTDEEKVAI AELIDVLKIE EAADKLQSAI
FNAAKKNGVQ PGNFFKTLYA ILLGASQGPK LGPYLLAMGK QNVIEALRRA LDQS
//
