SYK_METKA
ID SYK_METKA Reviewed; 555 AA.
AC Q8TWP6;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; OrderedLocusNames=MK0986;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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:0000255|HAMAP-Rule:MF_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR EMBL; AE009439; AAM02199.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TWP6; -.
DR SMR; Q8TWP6; -.
DR STRING; 190192.MK0986; -.
DR EnsemblBacteria; AAM02199; AAM02199; MK0986.
DR KEGG; mka:MK0986; -.
DR PATRIC; fig|190192.8.peg.1033; -.
DR HOGENOM; CLU_025562_1_0_2; -.
DR OMA; DWPMRWA; -.
DR Proteomes; UP000001826; 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 Gene3D; 6.10.20.10; -; 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 PANTHER; PTHR37940; PTHR37940; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00467; lysS_arch; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..555
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152754"
FT MOTIF 37..45
FT /note="'HIGH' region"
FT MOTIF 301..305
FT /note="'KMSKS' region"
SQ SEQUENCE 555 AA; 63462 MW; A06B1DF2DB4B8E80 CRC64;
MTKEHWSEVK AREVTEHCRK HADELPDEIV VASGASTSGR LHVGNARDVL TADAVARVLR
ERYHEDVRVV WISDDVDPLR RIPRDLDGRL SEDYLGVPYK AIPVGDEPYS DRWARNFVEE
LREFGAEVEW ISSAELYTDN GFVKLVREVV NDYYGGGGRL ASVLERFGLE DARVYMPVCE
ECGRIATTRV VDVDGWRIEY VCEGRHEIGD AVLEGCGHRG ELDLRKPIEV NGFEIPPGKL
GWKIEWPTRW VYLGVACEPF GKDHYVAGGS YEVGSAIAEE FFGFPAPVPV PYEWITLDGK
AMSSSKGHYV TLSDWGEVCH REVLRYLVLR GKPLKHLDLD LRFGLLQAVD DYDELEKRYF
AGEADERERR IYELSRVDEI PEECPPHVPF RFCAVVAQVV GIEDDVSEEE FERALEIFRR
TGHLEAEPEG FGREWLRERL EKASRWVDRY APEEARFRVR EEPEPVELSD KEREFLEDLV
RRLESETTKE DPETLQRTVF EAARTAGLRP ADAFRVFYNV VVGKDRGPRA GTLIAAVGVD
RISRLIRGCL EASED