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Database: UniProt
Entry: A0A194PZF4_PAPXU
LinkDB: A0A194PZF4_PAPXU
Original site: A0A194PZF4_PAPXU 
ID   A0A194PZF4_PAPXU        Unreviewed;       578 AA.
AC   A0A194PZF4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=RR46_04674 {ECO:0000313|EMBL:KPI98701.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI98701.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPI98701.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI98701.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPI98701.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(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}.
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DR   EMBL; KQ459583; KPI98701.1; -; Genomic_DNA.
DR   RefSeq; XP_013168377.1; XM_013312923.1.
DR   AlphaFoldDB; A0A194PZF4; -.
DR   STRING; 66420.A0A194PZF4; -.
DR   GeneID; 106118294; -.
DR   OrthoDB; 648039at2759; -.
DR   Proteomes; UP000053268; 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:0000313|EMBL:KPI98701.1};
KW   Ligase {ECO:0000313|EMBL:KPI98701.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053268}.
FT   DOMAIN          228..556
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..578
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        487..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   578 AA;  65482 MW;  A026AE584F8828B4 CRC64;
     MAEAPSEKLS KNELKRRMKA EQKLKEKAEK AAQQPAPTVE KKSTKPDEEI SPNEYYKIRS
     AAVAALKSGE REDHPYPHKF TVTTSLEGFI DKYNSLNSGE ILENVTVSVA GRIHSIRESG
     AKLIFYDLRA EGVKIQVMAN AKMYESEEKF VKDTDKLGRG DIIGCVGHPG KTKKGELSII
     PKTIKLLSPC LHMLPHLHFG LKDKETRFRK RYLDLILNDK VRQTFYTRAK IISYIRRFLD
     TMGFLEIETP MMNMIAGGAT AKPFVTHHND LNMDLYMRIA PELYHKMLVV GGLDRVYEIG
     RQFRNEGIDL THNPEFTTCE FYMAYADYND LITITETMIS GMVKSIHGSY KVTYHPDGPE
     GNEVEIDFTP PFARMPMIAT LEKVLGVKLP PADKLDTPEA NALLSELCVK HEVECPPPRT
     TARLLDKLVG EFLEDKCINP TFILDHPQIM SPLSKYHREI PGLTERFELF VMKKEICNAY
     TELNDPATQR ERFEQQAKDR AAGDDETPPT DEAFCTALEY GLPPTAGWGL GVDRFTMFMT
     DSNNIKEVLL FPAMKPDDPN KHHNENEPEG SSVQNGTQ
//
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