ID   TILS_STAPU              Reviewed;         493 AA.
AC   Q32RX0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
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};
OS   Staurastrum punctulatum (Green alga) (Cosmoastrum punctulatum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC   Desmidiales; Desmidiaceae; Staurastrum.
OX   NCBI_TaxID=102822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequences of the charophycean green algae
RT   Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT   extensive changes during the evolution of the Zygnematales.";
RL   BMC Biol. 3:22-22(2005).
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; AY958085; AAX45766.1; -; Genomic_DNA.
DR   RefSeq; YP_636406.1; NC_008116.1.
DR   AlphaFoldDB; Q32RX0; -.
DR   SMR; Q32RX0; -.
DR   GeneID; 4108639; -.
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..493
FT                   /note="tRNA(Ile)-lysidine synthase, chloroplastic"
FT                   /id="PRO_0000277071"
FT   BINDING         68..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   493 AA;  58834 MW;  541FCC83DC91FA7C CRC64;
     MQNNKDNYLK FTKMDKKSIR APYDQNDLSK KIQRIKKRED IFLLYKINNI ITEHTLLQPK
     QRILIAVSGG QDSICLLRIL FDLQRKWSWK LGIIHCDHRW NSRSKIQAEH VACLAINLQI
     NYHEGIAIES VQKESIARLW RYNVIQSVAI SNNYTAIITG HNASDRIETL LYNLMRGSGL
     HGLQSIKWKR NLCFSHFTRS VLSKIKFSFL VKKLKFIKTF MDHEDFQGNH FFFLKKRKQL
     HLIRPFLETT RTEIRNILTI WNFPSWPDVS NKELRIRRNR IRHRVIPYIR IHYNPNIDQT
     LVRWAEIVQS ETFYLEQLTN YILFKIEIKK KISSISLKIP LEQLRKQKEP SEEKLNFYQS
     AIPVDLLRSL PVAIQRRVLK QYIYINTNRI LGFQYIEQIR LSCLFSLQDS LRKFLHRHRC
     RPIYLSEHIS THSMKSSTSD TCIDWKGPKE KKKLVTPWLI FPGGIKFLIR KNYLFIFSPK
     NSSLTIKRPR IEQ