ID   TILS_NEPOL              Reviewed;         367 AA.
AC   Q9T390;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=tRNA(Ile)-lysidine synthase, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000255|HAMAP-Rule:MF_01161}; Synonyms=ycf62;
OS   Nephroselmis olivacea (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC   Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX   NCBI_TaxID=31312;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-484 / S-N-5-8;
RX   PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT   olivacea: insights into the architecture of ancestral chloroplast
RT   genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
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       {ECO:0000255|HAMAP-Rule:MF_01161}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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:0000255|HAMAP-Rule:MF_01161}.
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DR   EMBL; AF137379; AAD54930.1; -; Genomic_DNA.
DR   EMBL; AF137379; AAD54859.1; -; Genomic_DNA.
DR   RefSeq; NP_050888.1; NC_000927.1.
DR   RefSeq; NP_050959.1; NC_000927.1.
DR   AlphaFoldDB; Q9T390; -.
DR   SMR; Q9T390; -.
DR   PRIDE; Q9T390; -.
DR   GeneID; 801973; -.
DR   GeneID; 802039; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProt.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR   PANTHER; PTHR43033; PTHR43033; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Ligase; Nucleotide-binding; Plastid;
KW   tRNA processing.
FT   CHAIN           1..367
FT                   /note="tRNA(Ile)-lysidine synthase, chloroplastic"
FT                   /id="PRO_0000181820"
FT   BINDING         64..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   367 AA;  42863 MW;  CA13569ADE8F28BD CRC64;
     MKGGRVQVIT KNNSIAKHQL GEYAVHIYVL LYYLSMREIL REFEEACLLQ GLVSPSTRLL
     ISCSGGQDSV TLLFLLCQLQ TNWTWRLGVV YCNHMWRYGS IETPAKLARI CLLFGVSCSF
     SVSGSRLQKE EEGRSWRLRV LCRMSSIHSW FYISTGHTAS DRIETLLSNV LRGSSSSGMR
     SINWYTSLDT QVGHRRISIP IIRPLLGISR LELRNYANRW KLPLCYDPSN QDQRIRRNRI
     RHELLPYLRH WWNPQIDRLL AQTAEVTSWE SSYYDLICTQ ICQQYEWIGD GGVRFPWRIF
     HSIPTSLHSR ILWIFLNRAL VFLNPAHGFQ GNFDILQFLL ETKTCHCRHG SIYISKDVDW
     LRMTLVK