TILS_DEIRA
ID TILS_DEIRA Reviewed; 582 AA.
AC Q9RV23;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=tRNA(Ile)-lysidine synthase {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}; OrderedLocusNames=DR_1207;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(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: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF10777.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF10777.1; ALT_INIT; Genomic_DNA.
DR PIR; F75424; F75424.
DR RefSeq; NP_294931.1; NC_001263.1.
DR AlphaFoldDB; Q9RV23; -.
DR SMR; Q9RV23; -.
DR STRING; 243230.DR_1207; -.
DR PRIDE; Q9RV23; -.
DR EnsemblBacteria; AAF10777; AAF10777; DR_1207.
DR KEGG; dra:DR_1207; -.
DR PATRIC; fig|243230.17.peg.1406; -.
DR eggNOG; COG0037; Bacteria.
DR eggNOG; COG0590; Bacteria.
DR InParanoid; Q9RV23; -.
DR OMA; PTNQDPA; -.
DR OrthoDB; 666797at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; 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:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:UniProtKB-UniRule.
DR CDD; cd01992; PP-ATPase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR012796; Lysidine-tRNA-synth_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR028883; tRNA_aden_deaminase.
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; PF14437; MafB19-deam; 1.
DR Pfam; PF11734; TilS_C; 1.
DR SMART; SM00977; TilS_C; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW tRNA processing.
FT CHAIN 1..582
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181686"
FT DOMAIN 402..525
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 548..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ SEQUENCE 582 AA; 62706 MW; 0F8A84B1B75DEA13 CRC64;
MSLFHLLRRS VTVAVMSESA PNHTSARRLT QPLEPFVGRQ VLVGVSGGAD SVGLLRALLA
VGALPAVAHL DHALRPESVD DAAWVSDLCA RLGVPCEVTR IDVGAVAARR NWNLEAARRL
RYDVLSRAAK HSGAEVILTA HTRRDQAETV LMELLRGEGR IRGIPPQRGR VRRPWLNVGR
AEIETYLRGL GQDWREDASN ADPRFTRAWL RREVMPVLLT RFPAAETALA QVAELGAEDD
AALQALAARL TPHTPLDRQP PAVLRRWLAA ELRSGGLDFT AEQLRDLAGA LNAGQTRHLT
LPTGRDVTVT GGHLYTAPCD WPEPDFPLPP DWTRRTRQAG DRIRLAGGTR KLSDVLTDAH
LPRAERDRVP LLTDEHGAVQ WVGVQPPLWA VGARESLGLP ADPLHAAMGE ALALAQQAAE
RQEVPVGAVV LNADGEIVGR GRNTSREDGD MTCHAELAAL REAAAGLGTP YLSDCTLVVT
LEPCPMCLGA ALEARIGHIV YGAANPKAGA LGGVSDLLAD HWGWRPTVQG GVRAGEAARL
LREVFGEVRR RSADTPQTPN AETPAPRSSR STSASGKPTM LE
