ID   TILS_ZYGCR              Reviewed;         420 AA.
AC   Q32RJ9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
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   Zygnema circumcarinatum (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC   Zygnematales; Zygnemataceae; Zygnema.
OX   NCBI_TaxID=35869;
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; AY958086; AAX45881.1; -; Genomic_DNA.
DR   RefSeq; YP_636527.1; NC_008117.1.
DR   AlphaFoldDB; Q32RJ9; -.
DR   SMR; Q32RJ9; -.
DR   PRIDE; Q32RJ9; -.
DR   GeneID; 4108201; -.
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..420
FT                   /note="tRNA(Ile)-lysidine synthase, chloroplastic"
FT                   /id="PRO_0000277072"
FT   BINDING         63..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   420 AA;  48945 MW;  BEA497C8392FA6E2 CRC64;
     MLTNPIFYLT NSNTSKASTH SNTNSKSLFN TKREDLQILY KLNQLLIEKS ILHPYQRILI
     AVSGGQDSIC LLNILNKLRS TWHWKLGIVH CDHKWYLDSA LQAIHVSRLA ANMQIDLYQA
     LTTQSVNNEQ LARNWRYELI RHVAICHNFS VIVTGHTASD RVETLIYNLI RGSGISGLQS
     ISWKRKLNSM LTIRMRSVEE QIILYSKHVK CYQNRENLLE DKKNVDIYLI RPLLNVSRME
     LKHLVQNWKL SIWSDCSNQN ISICRNRIRH QLLPYLRQYF HPKIDYVLNS CTEVMYTETL
     YLDSIARYVL SKALSFISMP LNDQTCVKLD FELLRAVPLA IQRRILKYFL DVITHTSVSF
     KHVEQVRIAC LITTNSSNQF AKDSMNFTDQ LLINRSIYLP GKKILQVINA RFLIICNNIT