ID G1CCJ6_ANTPE Unreviewed; 579 AA.
AC G1CCJ6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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};
OS Antheraea pernyi (Chinese oak silk moth) (Bombyx pernyi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Saturniinae; Saturniini; Antheraea.
OX NCBI_TaxID=7119 {ECO:0000313|EMBL:AEB77710.1};
RN [1] {ECO:0000313|EMBL:AEB77710.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Shenhuang No.1 {ECO:0000313|EMBL:AEB77710.1};
RA Liu Y.Q., Qin L.;
RT "Molecular cloning, expression pattern, and phylogenetic analysis of the
RT lysyl-tRNA synthetase gene from the Chinese oak silkworm Antheraea
RT pernyi.";
RL (In) Brown, G.G. (eds.);
RL MOLECULAR CLONING - SELECTED APPLICATIONS IN MEDICINE AND BIOLOGY,
RL pp.267-276, InTech, New York, NY, USA (2011).
RN [2] {ECO:0000313|EMBL:AEB77710.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Shenhuang No.1 {ECO:0000313|EMBL:AEB77710.1};
RA Kumar K., Prasad M.;
RT "Molecular cloning and characterization of a novel 14-3-3-like gene from
RT foxtail millet (Setaria italica L.).";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; JF773568; AEB77710.1; -; mRNA.
DR AlphaFoldDB; G1CCJ6; -.
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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:AEB77710.1};
KW Ligase {ECO:0000313|EMBL:AEB77710.1}.
FT DOMAIN 227..555
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 65623 MW; 58DAB262154AF1BE CRC64;
MAETSSEKVS KNELKRRLKA EQKLKEKAEK VAQQPVQPAT EKKISKQEEE ISPNEYYKLR
SAAVAALKTG AKEEHPYPHK FTVTISLEEF INKYNNLNSG EVLENTTVSL AGRVHSIRES
GAKLIFYDLR AEGVKIQVMA NAKLYESEFE TDTDKLRRGD IIGCIGHPGK TKKGELSIVP
QSIKLLSPCL HMLPHLHFGL KDKETRFRKR YLDLILNDQV RQTFYTRAKI IAYVRRFLDN
MGFLEIETPM MNMIPGGATA KPFITHHNDL NMDLFMRIAP ELYHKMLVVG GLDRVYEIGR
QFRNEGIDLT HNPEFTTCEF YMAYADYNDL ITITETMLSG MVKSIHGTYK VKYHPDGPSG
EEVEIDFTPP FARVPMIATL EKVLNVKLPS PDKLDTAEAN SLLSQLCEKH EVECPPPRTT
ARLLDKLVGE FLEDKCINPT FILDHPQIMS PLSKYHRDIP GLTERFELFV MKKEICNAYT
ELNDPATQRE RFEQQAKDRA AGDDETPPTD EAFCTALEYG LPPTAGWGLG VDRLTMFLTD
ANNIKEVLLF PAMKPDDPNK HNNEEGNAAD STPLLQNGA
//
