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Database: UniProt
Entry: A0A0L0BZK1_LUCCU
LinkDB: A0A0L0BZK1_LUCCU
Original site: A0A0L0BZK1_LUCCU 
ID   A0A0L0BZK1_LUCCU        Unreviewed;       606 AA.
AC   A0A0L0BZK1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00015745, ECO:0000256|RuleBase:RU003748};
DE            EC=6.1.1.6 {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU003748};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563, ECO:0000256|RuleBase:RU003748};
GN   ORFNames=FF38_00889 {ECO:0000313|EMBL:KNC25507.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC25507.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC25507.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC25507.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC25507.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
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:0000256|ARBA:ARBA00000204,
CC         ECO:0000256|RuleBase:RU003748};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNC25507.1}.
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DR   EMBL; JRES01001107; KNC25507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0BZK1; -.
DR   STRING; 7375.A0A0L0BZK1; -.
DR   EnsemblMetazoa; KNC25507; KNC25507; FF38_00889.
DR   OMA; EIFGEKC; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00499; lysS_bact; 1.
DR   PANTHER; PTHR42918:SF9; LYSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037069}.
FT   DOMAIN          256..587
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          22..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  69059 MW;  103B170665B095ED CRC64;
     MAESGQISKN VKRHVFQSTT TLFHASTSLQ QPSKKTKLEL KRRLKAEQKA KEKAEKEANK
     VATAPAASGE GKKKSAASEE EISPNEYFKL RTAAVAELKK SPETDPYPHK FHVSISLENY
     INKYTNLKDG EMLENEQLSI AGRVHAIRES GAKLIFYDLR GEGVKLQVMA NAKLYKSEKD
     FEVDTGKIRR GDIIGINGFP AKTKKGELSI VPKEIKLLSP CLHMLPHLHF GLKDKETRFR
     QRYLDLILNN KVRETFQIRA KIISYVRQFL DRMGFLEIET PMMNMIAGGA TAKPFITHHN
     DLNMDLYMRI APELYHKMLV VGGLDRVYEI GRQFRNEGID LTHNPEFTTC EFYMAYADYH
     DLIEMTEQMV SGMVKAIHGT YKIKYHPEGP EGPEEEIDFT PPFKRVSMIK TLEEKLNVKF
     PSATTLNTKE TNEFLSQLCI KHNVECPAPR TTARLLDKLV GEFIEETCIN PTFICEHPQI
     MSPLAKYHRS EPGLTERFEL FVMKKEVCNA YTELNDPMVQ RERFEQQASD KAAGDDEAQL
     VDENFCTALE YGLPPTGGWG MGIDRLTMFL TDANNIKEVL LFPAMKPDDP NRAHPAELNN
     AEEQKQ
//
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