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Database: UniProt
Entry: A0A077ZVR9_STYLE
LinkDB: A0A077ZVR9_STYLE
Original site: A0A077ZVR9_STYLE 
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
//
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