ID   TILS_HELSJ              Reviewed;         280 AA.
AC   Q2EEX9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=tRNA(Ile)-lysidine synthase, plastid;
DE            EC=6.3.4.19;
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase;
DE   AltName: Full=tRNA(Ile)-lysidine synthetase;
GN   Name=tilS; Synonyms=ycf62;
OS   Helicosporidium sp. subsp. Simulium jonesii (Green alga).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium; unclassified Helicosporidium.
OX   NCBI_TaxID=145475;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16630350; DOI=10.1186/1741-7007-4-12;
RA   de Koning A.P., Keeling P.J.;
RT   "The complete plastid genome sequence of the parasitic green alga,
RT   Helicosporidium sp. is highly reduced and structured.";
RL   BMC Biol. 4:12-12(2006).
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC       the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC       ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC       the amino acid specificity of the tRNA from methionine to isoleucine
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC         diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC         Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC         ChEBI:CHEBI:456215; EC=6.3.4.19;
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC       motif, predicted to be a P-loop motif involved in ATP binding.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ398104; ABD33964.1; -; Genomic_DNA.
DR   RefSeq; YP_635915.1; NC_008100.1.
DR   AlphaFoldDB; Q2EEX9; -.
DR   SMR; Q2EEX9; -.
DR   GeneID; 4100407; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR   GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProt.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   PANTHER; PTHR43033; PTHR43033; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Plastid; tRNA processing.
FT   CHAIN           1..280
FT                   /note="tRNA(Ile)-lysidine synthase, plastid"
FT                   /id="PRO_0000296326"
FT   BINDING         28..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   280 AA;  33401 MW;  85729A0AC16DFE7A CRC64;
     MLKNIIYSYI TQLKNLLSKK LNVLCTFSAG QDSFFLLYCL IHIISNKNNK IKLQHNHHFL
     QSSNILSFWQ CIKVASIFKI PLVINLLEIN LANKDFMTEN EARKWRYDSF LRNSLFQNEK
     PSIFIGHTGS DLLETFFWHF LRNSIIDYQL IKKKLLWNIP YYISNFSSVG YKNSSKVKIK
     LTNKKKKINC LINHNLMLNK AKKSFLKKDL TQLVLITRPL VNLHRQDIFL FRKNLKLPVI
     TDKSNDNNYY YRNRIRNILF PIMRILFNKK TDKNLIKLFL