SYK_AERPE
ID SYK_AERPE Reviewed; 545 AA.
AC Q9YFT9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 112.
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=APE_0161.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA79072.2; -; Genomic_DNA.
DR PIR; F72771; F72771.
DR AlphaFoldDB; Q9YFT9; -.
DR SMR; Q9YFT9; -.
DR STRING; 272557.APE_0161.1; -.
DR EnsemblBacteria; BAA79072; BAA79072; APE_0161.1.
DR KEGG; ape:APE_0161.1; -.
DR PATRIC; fig|272557.25.peg.115; -.
DR eggNOG; arCOG00485; Archaea.
DR BRENDA; 6.1.1.6; 171.
DR Proteomes; UP000002518; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..545
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152746"
FT MOTIF 33..41
FT /note="'HIGH' region"
FT MOTIF 288..292
FT /note="'KMSKS' region"
SQ SEQUENCE 545 AA; 63089 MW; 61D5B616F7BC5D50 CRC64;
MPVHWVDKLV AELEAKLQNR GKDEYIFNGG LSVSGLQHIG RLRGEVLLGE AVRRELEKRG
FRVKQLLTLY TVDPWKGKDE QRREFPDPKA AERYVGWPLD RVPDPKGCHA SWVDHFWSDF
GPYIGVFTDG KIEVVTTREL YKGRLKEFIT TMVLPRRDEI RRVINKYRGR KPYQEGWIPL
EPRCARCGRI DSTEALEILG GERVRYRCSY CGYQGESSIE DSKLNWRIEW AGVWWSLGVD
FEPYGKDHAT PGGSRDSAAE LARLLGFEPP EGVWYEWVSL RAGGREADMS SSGFTGITPR
EWLDIAHPQI LRFIYFLHPP TRRVVVDLSE IPSYYSQYYR AERIYFGIEE ASTVEETRYL
ARTYELSHPS NPPAKPPSQI PYSHAAIVAQ VVGPERLWTD GLERLKRAGL LGHDEYSIRW
AKELLEKAYK WARRYAPKHL KFEIPDSPPE DALRRIEKPD LLEKLAEVLE SVEEWSEERI
KQALVEFGEG MSSSERRRFY RDFYLAIVGR PEGPRAAPLL SLMDRGFVVD RLRKAANLSR
ELKGR