(data stored in ACNUC1104 zone)

SWISSPROT: TILS_RHOE4

ID   TILS_RHOE4              Reviewed;         325 AA.
AC   C0ZNS6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
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};
GN   OrderedLocusNames=RER_06200;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34
CC       of the AUA codon-specific tRNA(Ile) that contains the anticodon
CC       CAU, in an ATP-dependent manner. Cytidine is converted to
CC       lysidine, thus changing the amino acid specificity of the tRNA
CC       from methionine to isoleucine. {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-
CC         COMP:10670, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:82748,
CC         ChEBI:CHEBI:83665, ChEBI:CHEBI:456215; EC=6.3.4.19;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; AP008957; BAH31328.1; -; Genomic_DNA.
DR   RefSeq; WP_020906067.1; NC_012490.1.
DR   SMR; C0ZNS6; -.
DR   STRING; 234621.RER_06200; -.
DR   PRIDE; C0ZNS6; -.
DR   EnsemblBacteria; BAH31328; BAH31328; RER_06200.
DR   KEGG; rer:RER_06200; -.
DR   PATRIC; fig|234621.6.peg.1067; -.
DR   eggNOG; ENOG4107RD1; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000236508; -.
DR   KO; K04075; -.
DR   OMA; DPHNADP; -.
DR   Proteomes; UP000002204; Chromosome.
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: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; 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   InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF09179; TilS; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0ZNS6.
DR   SWISS-2DPAGE; C0ZNS6.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   tRNA processing.
FT   CHAIN         1    325       tRNA(Ile)-lysidine synthase.
FT                                /FTId=PRO_1000213717.
FT   NP_BIND      34     39       ATP. {ECO:0000255|HAMAP-Rule:MF_01161}.
SQ   SEQUENCE   325 AA;  34603 MW;  2E5834D863416A52 CRC64;
     MLLPETPALL ALRQAVRAWT VAFEPRRRVV VALSGGADSL ALTAAAVAET DSVDALIVDH
     RLQPGSDAVA RSAADQALAL GCRTATVLTV DVAEGGSLEA AAREARYSAL RDARTDLPVL
     LGHTLDDQAE TVLLGLSRGS GGRSIQGMAA FDAPWGRPLL GIRRSVTRAA CVDLGITPWE
     DPHNNNPEFT RVRLRHEALP LLEEILGGGV AEALARTATQ LREDGEALDE YAEALLLRAV
     VDGEVEVDTL AEAPTAIRRR ALRAWLLQGG AKALTDKQLR AVDALVIDWR GQGGVAIGGG
     TPEARLVAAR RRGRLILGFE DRRRV
//

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