SYK_THEAC
ID SYK_THEAC Reviewed; 507 AA.
AC P57677;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS; OrderedLocusNames=Ta1163;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL445066; CAC12288.1; -; Genomic_DNA.
DR AlphaFoldDB; P57677; -.
DR SMR; P57677; -.
DR STRING; 273075.Ta1163; -.
DR PRIDE; P57677; -.
DR EnsemblBacteria; CAC12288; CAC12288; CAC12288.
DR KEGG; tac:Ta1163; -.
DR eggNOG; arCOG00485; Archaea.
DR HOGENOM; CLU_025562_1_0_2; -.
DR OMA; DWPMRWA; -.
DR Proteomes; UP000001024; Chromosome.
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; -; 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; IPR001412; aa-tRNA-synth_I_CS.
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 PANTHER; PTHR37940; PTHR37940; 1.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00467; lysS_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..507
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152762"
FT MOTIF 26..34
FT /note="'HIGH' region"
FT MOTIF 270..274
FT /note="'KMSKS' region"
SQ SEQUENCE 507 AA; 58119 MW; 59DC4C8275C0DA6B CRC64;
MISLFWADAL VKDLSGPQRV STGISPSGPI HVGNMREILT GDILFKAITK RGLESDFIYL
CDDMDPLRKV YPFLSKDYER YVGQPLKNIP APQGAGKYSD YYLEPFVRVM KEANIPARVI
KTSDLYESGM LAQACDIAIN NREKIKDILE TVSGRKIEGD FYPYEPLCEK CGRISTTHVI
SYSYPYAEYA CKCGHHGFAD IRKAEGKMPW RVEWPAKWFA LKVTVEPFGK DHGAPGGSYD
TGRRIAREVF GIEPPVPLMY ERIILKGKGA MHSSTGLAIA ASEIMEVIPP DLLRYMIARV
NPGRHIDFDP GMGILALSDE LEKLQDAYFE NRASLDEDQA AMVEYSLVNK DRKPYPVDFR
HLVTLVQIYR TEDEILRAVK KGQPSDFIEA DFRKEIEYAR RWLERYAPES VKFRILPVDQ
KIELSDSDLA ILSDFLNGIE DMPWNSESIH DRIYEISQKF KTNPESVFTL FYRVFIGKDR
GPRLGYFLFN LGKDFVRERI RNVIRDH
