ID   TILS_THET8              Reviewed;         507 AA.
AC   Q5SI38;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=tRNA(Ile)-lysidine synthase;
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; OrderedLocusNames=TTHA1542;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm {ECO:0000250}.
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; AP008226; BAD71365.1; -; Genomic_DNA.
DR   RefSeq; WP_011228750.1; NC_006461.1.
DR   RefSeq; YP_144808.1; NC_006461.1.
DR   AlphaFoldDB; Q5SI38; -.
DR   SMR; Q5SI38; -.
DR   STRING; 300852.55772924; -.
DR   PRIDE; Q5SI38; -.
DR   EnsemblBacteria; BAD71365; BAD71365; BAD71365.
DR   GeneID; 3169806; -.
DR   KEGG; ttj:TTHA1542; -.
DR   eggNOG; COG0037; Bacteria.
DR   eggNOG; COG0590; Bacteria.
DR   HOGENOM; CLU_018869_0_1_0; -.
DR   OMA; PTNQDPA; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
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   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..507
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_0000181793"
FT   DOMAIN          370..500
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   BINDING         24..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         445
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         448
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   507 AA;  56308 MW;  617E79E01C69D0B9 CRC64;
     MDVPAFRERL LRLAPKDPLV LAVSGGGDSV ALALLVKEAG RQAVVAHLDH GLRPESPLDQ
     AFVRALAERL GFPFFTERVE VARIAQARGE NLEAVAREVR YAFLHRVARE VGARAILTAH
     TLDDQAETVL LQLLQGTARA TGIREREGIV VRPLLAHTRE ELRAYLRARG EAWREDPTNQ
     DPALDRNFLR LFVFPLLEER FPAAKRALAR FAEARAEEEG VLERQAEARL LPDPRFFVPA
     FRAAPLLEAP LAVRRRALRR LLEKLGLRPE ARLVLLLEEA LRGRPQTLPG GVLARRKGGT
     LFLLPPRPRL PLPPGFRRPA PGDYLERPSG RKRLVDFLAE KGVPRELKPL WPVRAEGNRV
     VEVLGLYPPP PEEAHMAEAL AEAASAFREG EVPVGAVLVL PGRVLRAHNR VEGLRDPTAH
     AEMLLLREAG PEARGGRLYV TLEPCLMCHH ALAQAGVEVV YGAENLKEGA LTRFGLPTRA
     RGGVRERECA KLLRDFFARL REGCRSG