ID A0A166CWX7_9EURY Unreviewed; 529 AA.
AC A0A166CWX7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ECO:0000313|EMBL:KZX17357.1};
GN ORFNames=MBFIL_01990 {ECO:0000313|EMBL:KZX17357.1};
OS Methanobrevibacter filiformis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=55758 {ECO:0000313|EMBL:KZX17357.1, ECO:0000313|Proteomes:UP000077066};
RN [1] {ECO:0000313|EMBL:KZX17357.1, ECO:0000313|Proteomes:UP000077066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11501 {ECO:0000313|EMBL:KZX17357.1,
RC ECO:0000313|Proteomes:UP000077066};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter filiformis DSM 11501.";
RL Submitted (APR-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: 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:KZX17357.1}.
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DR EMBL; LWMT01000025; KZX17357.1; -; Genomic_DNA.
DR RefSeq; WP_066970602.1; NZ_LWMT01000025.1.
DR AlphaFoldDB; A0A166CWX7; -.
DR STRING; 55758.MBFIL_01990; -.
DR PATRIC; fig|55758.3.peg.221; -.
DR OrthoDB; 6838at2157; -.
DR Proteomes; UP000077066; 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}; Reference proteome {ECO:0000313|Proteomes:UP000077066}.
FT DOMAIN 448..526
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 28..36
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 272..276
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 529 AA; 61601 MW; 4EA8BE403BB0DB9A CRC64;
MKHWIERIAD ELKERDVEKH VIASGTSISG SIHIGNSCDV FIANAIGKKL KELGVNAETI
WIADDHDPLR KVPYPLPESY DKYLGMPYSN IPCPEGCCSS FVEHFEKPLF DVLDDFGIEL
TPKSGFEMYK QGLYNDYIRI SLEKAEEIRN IFNQYREHPL ANDWLPYNPI CDECGRVNTT
YAYAFNEDTV QYRCDCGHDG EMDINSGNGK LTWRVEWAAR WKIFKITCEP FGKDHAASGG
SYDVSSIISK EIFNYTAPYP VPYEWITLDG EAMSKSKGVF FTPKQWLEIA PAESLNYFLF
RSKPMKHKDF SPKMAFLDFI EQFDKVEKVY YNEEEAPSEK EDKKFRKIYE MSKIQENTEK
TNLPFRPPYR FLTVAYQIAG EDNEKIFEIL KKNSQLTDSF KNKEYETLSE IENEYFEKRV
DEVKNWLEKY APKFVKFQVM KNIPNLPLTD EQTTFLKELA ILIEENDFND AAKLHDEMYE
ILNKQGLKIQ KAFQAIYKVV LGQKQGPKAA SFLLSLDKDF VVKRLKLLE
//
