SYK_PICTO
ID SYK_PICTO Reviewed; 504 AA.
AC Q6L1V1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=PTO0466;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43051.1; -; Genomic_DNA.
DR RefSeq; WP_011177267.1; NC_005877.1.
DR AlphaFoldDB; Q6L1V1; -.
DR SMR; Q6L1V1; -.
DR STRING; 263820.PTO0466; -.
DR EnsemblBacteria; AAT43051; AAT43051; PTO0466.
DR GeneID; 2844802; -.
DR KEGG; pto:PTO0466; -.
DR PATRIC; fig|263820.9.peg.492; -.
DR eggNOG; arCOG00485; Archaea.
DR HOGENOM; CLU_025562_0_0_2; -.
DR OMA; DWPMRWA; -.
DR OrthoDB; 9880at2157; -.
DR Proteomes; UP000000438; 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..504
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000259352"
FT MOTIF 23..31
FT /note="'HIGH' region"
SQ SEQUENCE 504 AA; 58004 MW; AA3528A01868E8D5 CRC64;
MHWSESLLKD VSGDQRISTG ISPSGPIHIG NMREILTGDI IYKEALKLGI KASFIYLCDD
MDPLRKVYPF LPGSYERYVG HPLSMIPAPD GDKTYSEYFL EPFKETIDKI DVRPEIISTT
SLYKNGVLSR AIDIAMNNRE KIKNILNSIG NYKITGDWYP YEPVCKSCGR INTTTVISYN
YPYAEYKCKC GYTGKADIRT DDGKMPWRVE WPAKWFSLHV TIEPFGKDHG AAGGSYDTGK
AIASDIFNIN PPLPLLYERI FLKGKGVMHS STGVVIPASE MIKFSPPEII RFLIAKNNPG
RHIDFDPGPG LLNLIDEYEK YERAYFGLDS VKDDDYKEVY ELSRLKILKE PEKITFRHIV
TLVQIYNNND ALLSALKRSG YEKDYIDDYI MNEIDTARYW LEKYAPPEMK FSLTDENINL
NDDERKIVNE FLENIDNIEW SPDSIHNYVY DIIGRSKMRP QDAFAVFYKI LIGRSRGPRL
GYFIYNLGRE YIIKRFSSIL AETF