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Database: UniProt
Entry: A0A444XEC1_ARAHY
LinkDB: A0A444XEC1_ARAHY
Original site: A0A444XEC1_ARAHY 
ID   A0A444XEC1_ARAHY        Unreviewed;       606 AA.
AC   A0A444XEC1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00013166, 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=Ahy_B09g095340 {ECO:0000313|EMBL:RYQ87803.1}, DS421_19g642940
GN   {ECO:0000313|EMBL:QHN76330.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ87803.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYQ87803.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738}, and
RC   GDAAS-fuhuasheng2018 {ECO:0000313|EMBL:RYQ87803.1};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYQ87803.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QHN76330.1, ECO:0000313|Proteomes:UP000464620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Young leaf {ECO:0000313|EMBL:QHN76330.1};
RA   Zhuang W., Chen H., Varshney R., Wang D., Ming R.;
RT   "Genome sequence of Arachis hypogaea, cultivar Shitouqi.";
RL   Submitted (JAN-2020) 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};
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DR   EMBL; CP031001; QHN76330.1; -; Genomic_DNA.
DR   EMBL; SDMP01000019; RYQ87803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444XEC1; -.
DR   STRING; 3818.A0A444XEC1; -.
DR   OrthoDB; 5487299at2759; -.
DR   Proteomes; UP000289738; Chromosome b09.
DR   Proteomes; UP000464620; Chromosome b09.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
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; 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:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:QHN76330.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT   DOMAIN          257..600
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          41..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  67962 MW;  6E8610323F80A5D8 CRC64;
     MEALKLWNLT SQPLKRHLLH STTSITSYAF RRTPRTLLLR SSSSSSSSST ASSSAPDVDK
     PTGAASRTAG RNRRAPASPT TSTSDREAVR AIRLRKVEEL RSKGLDPYAY GWEKTHSANQ
     LQDIYRDLGN GEEANGENDH VSIAGRIVAR RAFGKLAFLT LRDDSGTIQL YCDKERLIDD
     QFEQLKAHVD IGDILGARGS IKRTEKGELS VCVLSFAILT KSLLPLPDKY HGLTDIDKRY
     RQRYVDMIAN PEVADVFRKR AKVVSEIRRT MDSLGYIEVE TPVLQGAAGG AEARPFITHH
     NSLGRDLYLR IATELHLKRM LVGGFEKVYE IGRIFRNEGI STRHNPEFTT IEMYEAYSDY
     QSMMNLAEEI VTQCALAVLG KLTLDYQGVE ICLERPWRRE TMHNLVKEVS GIDFSELGYD
     LEVAKKVTLS TLGNNLDAKD KASIEACQSV GHLLNEVFEV VVEPKLIQPI FVLDYPIEIS
     PLAKPHRRSI GLTERFELFI CGREIGNAFS ELTDPIDQRG RLEDQVRQHE KKRAEAASRN
     ADKKEGTENE DDLYEVTLDD DFLTALEYGM PPASGMGLGI DRIVMLLTNS PSIRDVIAFP
     VLKVQQ
//
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