ID A0A077ZVR9_STYLE Unreviewed; 591 AA.
AC A0A077ZVR9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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 Name=Contig7684.g8193 {ECO:0000313|EMBL:CDW73340.1};
GN ORFNames=STYLEM_2316 {ECO:0000313|EMBL:CDW73340.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW73340.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW73340.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW73340.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-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; CCKQ01002248; CDW73340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZVR9; -.
DR EnsemblProtists; CDW73340; CDW73340; STYLEM_2316.
DR InParanoid; A0A077ZVR9; -.
DR OMA; DFRNEGM; -.
DR OrthoDB; 648039at2759; -.
DR Proteomes; UP000039865; 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:CDW73340.1};
KW Ligase {ECO:0000313|EMBL:CDW73340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT DOMAIN 252..585
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 68282 MW; A72C0E2A0C44A37B CRC64;
MEATKNDKRQ QNKKEYQTKE ENGKTLYLDE PSGEYVSKNE IKTREKLREK EEKLKAKQDQ
KQIDQPADQK KKEVEMDPTQ YTENRKQWIQ SVRDKNENPY PHKFNRTHKL DEFHAAYNSK
CVENNVFIEE ETVAITGRVI SIRNSGAKLI FIDLQGDDNK VQIFANAANY TGEFDTLLAR
IKRGDIIGVE GQPGRTKTGE LSVRPTLITS LSYCLHQLPS QHTIDTKGLT KDTRFRQRYL
DLLTNPRTKK TFRVRNEVIN FIRNFLLELD FLEVETPMMN MIPGGATARP FETFHNDLNM
KLFMRIAPEL YLKMLIVGGI DRVFEIGKQF RNEGIDLTHN PEFTTCEFYW AYADYHDLMD
LTEKMLSQMA LKIHGSYKFQ YHPKGIEEKD NVIELDFTPP FRRIPMMKGL EEAVGVKLPA
ADTLHTDEAR EFFDKLAAEH KVKCGEPRTV ARLIDKLVGH FLEVNCKNPT FITDTPQIMS
PLAKWHRSEA GLSERFELFI NYHEIVNAYT ELNDPKVQLD FFSEQAKAKE LGDDEAQAID
ANFVTALEFG LPPTGGWGIG IDRLTMLMSD TNSIKEVLLF PAMKPDEQLE E
//