ID A0A0C7NB84_9SACH Unreviewed; 591 AA.
AC A0A0C7NB84;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=LALA0_S06e04544g {ECO:0000313|EMBL:CEP62818.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62818.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP62818.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62818.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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; LN736365; CEP62818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7NB84; -.
DR STRING; 1245769.A0A0C7NB84; -.
DR HOGENOM; CLU_008255_6_0_1; -.
DR OrthoDB; 648039at2759; -.
DR Proteomes; UP000054304; 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 Reference proteome {ECO:0000313|Proteomes:UP000054304}.
FT DOMAIN 251..579
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 67795 MW; 0E599AA6698888C2 CRC64;
MSQEEQVKGV NDAIANLHLD ETTGEMVSKS ELKKRIKQRQ TDAKKAAKKA SAQPKPEAKK
KANDAFADLD PSQYFEARSR QIQELKKTKS PNPYPHKFHV STALPAFLEK YSHLQRGETL
PEEKVSLAGR VHTKRESGSK LKFYVLHGDG VEVQLMSQVQ DYGDESAYEA DHDLIKRGDI
IGVEGYVGRT QPKKGGEGEI SVFVSRIQLL TPCLHILPAD HFGFKDQETR YRKRYLDLIM
NKNAKPRFIT RSKIISFIRR FLDERSFIEV ETPMMNVIAG GATAKPFVTH HNDLNMDMFM
RIAPELFLKE LVVGGMDRVY EIGRQFRNEG IDMTHNPEFT TCEFYQAYAD AYDLMDTTEM
MISEMVKEIT GSYVIKYHPD PQDPSKELEL NFTRPWKRIN MIEELESRLN VKFPPGDQLH
TAETGEFFKR VLKENKLECA PPLTNARMLD KLVGELEDTC INPTFIFGHP QMMSPLAKYS
RDKPGLCERF EVFVATKEIC NAYTELNDPF DQRNRFEEQA RQKDQGDDEV QLIDETFCNA
LEYGLPPTGG WGCGIDRLAM FLTDSNTIRE VLLFPTLKPD VQREVEDEKT N
//
