(data stored in SCRATCH zone)

SWISSPROT: Q6BMB5_DEBHA

ID   Q6BMB5_DEBHA            Unreviewed;       593 AA.
AC   Q6BMB5;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 111.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|RuleBase:RU003748};
DE            EC=6.1.1.6 {ECO:0000256|RuleBase:RU003748};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|RuleBase:RU003748};
GN   OrderedLocusNames=DEHA2F06820g {ECO:0000313|EMBL:CAG88988.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88988.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88988.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(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,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529,
CC         ChEBI:CHEBI:456215; EC=6.1.1.6;
CC         Evidence={ECO:0000256|RuleBase:RU003748};
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DR   EMBL; CR382138; CAG88988.1; -; Genomic_DNA.
DR   RefSeq; XP_460656.1; XM_460656.1.
DR   STRING; 4959.XP_460656.1; -.
DR   EnsemblFungi; CAG88988; CAG88988; DEHA2F06820g.
DR   GeneID; 2904128; -.
DR   KEGG; dha:DEHA2F06820g; -.
DR   HOGENOM; HOG000236577; -.
DR   InParanoid; Q6BMB5; -.
DR   KO; K04567; -.
DR   OMA; EIFGEKC; -.
DR   OrthoDB; 837479at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR   CDD; cd00775; LysRS_core; 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; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR034762; Lys-tRNA-ligase_II_bac/euk.
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   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMB5.
DR   SWISS-2DPAGE; Q6BMB5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN      251    581       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   593 AA;  67605 MW;  918EA408293DCFB7 CRC64;
     MSEEVAKVAE QLQKTYLDDV TGEQVSKTEL KKRQKQRAND AKKAEKAAKS AASAPKVAKK
     KDQLVDLNPN QYFEIRSRQI DELRQANLAD GSAFNPYPHK FHVSIQLPAF AEKYKDLKKG
     ESLKDVEVKV SGRIMGKRES GSKLKFYVLK GDGVQIQIMA QAQDVENAEE YEKMHEYLRR
     GDIIGVTGYP GRTSPAKGGE GEVSVFATSV QLLTPCLHML PTEHYGFKDQ EARYRKRYLD
     LIMNESTRDR FKVRSQIISF IRKFLDTRDF TEVETPMMNV IAGGATAKPF VTHHNDLNMD
     MFMRIAPELF LKELVVGGMD RVYEIGRQFR NEGIDMTHNP EFTTCEFYQA YADVYDLMDM
     TELLFSEMVK KITGDYKVTY HPEGPEGKAL TLDFTRPWKR VNMIEELEKV FNVTFPAGDQ
     LHTEETGKFL KQILIDHKLD CSPPLTNARM LDKLVGELED ASINPTFIFG HPQMMSPLAK
     KDRDNVGLCE RFEVFVATKE ICNAYTELND PFDQRQRFEE QARQKAQGDD EAQMVDETFC
     NALEYGLPPT AGWGCGIDRL AMFLTDSNTI REVLLFPTLK PDALVKGEET SDN
//

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