ID   SYKC_SCHPO              Reviewed;         591 AA.
AC   Q9UUE6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Lysine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   Name=krs1; ORFNames=SPBC17G9.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAB52801.1; -; Genomic_DNA.
DR   PIR; T39726; T39726.
DR   RefSeq; NP_595892.1; NM_001021799.2.
DR   AlphaFoldDB; Q9UUE6; -.
DR   SMR; Q9UUE6; -.
DR   BioGRID; 276298; 4.
DR   STRING; 4896.SPBC17G9.03c.1; -.
DR   iPTMnet; Q9UUE6; -.
DR   MaxQB; Q9UUE6; -.
DR   PaxDb; Q9UUE6; -.
DR   PRIDE; Q9UUE6; -.
DR   EnsemblFungi; SPBC17G9.03c.1; SPBC17G9.03c.1:pep; SPBC17G9.03c.
DR   GeneID; 2539746; -.
DR   KEGG; spo:SPBC17G9.03c; -.
DR   PomBase; SPBC17G9.03c; krs1.
DR   VEuPathDB; FungiDB:SPBC17G9.03c; -.
DR   eggNOG; KOG1885; Eukaryota.
DR   HOGENOM; CLU_008255_6_0_1; -.
DR   InParanoid; Q9UUE6; -.
DR   OMA; EIFGEKC; -.
DR   PhylomeDB; Q9UUE6; -.
DR   PRO; PR:Q9UUE6; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; ISS:PomBase.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; ISS:PomBase.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR034762; Lys-tRNA-ligase_II_bac/euk.
DR   InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PIRSF; PIRSF039101; LysRS2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..591
FT                   /note="Lysine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000315953"
FT   REGION          24..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  67494 MW;  0FE9069A0C27AAB9 CRC64;
     MSEEQVNGVT QAVKALVLDP VTGEQVSKTE LKKREKQRAR ELAKAKKQAE KAASAPVAAP
     KSSSKKEEDL DPSQYFENRS RTIMELRQTK DPNPYPHKFQ VTITLPEFIA KYEGLARGET
     KPEVEVAVAG RVLGLRTAGN KLRFYEIHAD GKKLQVMCQA QDADTVDFAA QHEHLRRGDI
     IGIRGYPGRS NPKGRADGEL SIFARQCVLL SPCLRMLPKE HYGLKDLEIR HRQRYLDLIM
     NRSTRDRFVM RSRIIQYIRH FFDSRDFMEV ETPMMNMIAG GATAKPFVTH HNDLDMDLYM
     RIAPELYLKM LVVGGLDRVY EIGRQFRNEG ADLTHNPEFT SIEFYQAYAD YYDLMDTTEE
     LLSGLVKDLT GSYKVPYHPE GPEGPKWELD FSRPWRRINM IEYLEEKLNT KFPPGDQLHT
     PEANAFLRDL CAKHGVECAP PQTCSRLLDK LVGEFIESEC INPTFIIGHP QMMSPLAKYH
     RSDAGLCERF EAFVATKEIC NAYTELNDIF DQRARFEEQA RQKAQGDDEA QIIDENFCTA
     LEYGLPPTGG WGMGVDRLVM FLTDSNTIRE VLLFPHMKPE VQAAEPTVVK E