(data stored in SCRATCH zone)

SWISSPROT: A1SDU8_NOCSJ

ID   A1SDU8_NOCSJ            Unreviewed;       321 AA.
AC   A1SDU8;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161, ECO:0000256|SAAS:SAAS00052161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161, ECO:0000256|SAAS:SAAS00994358};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000256|HAMAP-Rule:MF_01161};
GN   OrderedLocusNames=Noca_0441 {ECO:0000313|EMBL:ABL79983.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79983.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79983.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
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:0000256|HAMAP-Rule:MF_01161,
CC       ECO:0000256|SAAS:SAAS00557872}.
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:0000256|HAMAP-Rule:MF_01161,
CC         ECO:0000256|SAAS:SAAS01121949};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161,
CC       ECO:0000256|SAAS:SAAS00360206}.
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       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01161, ECO:0000256|SAAS:SAAS00994361}.
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DR   EMBL; CP000509; ABL79983.1; -; Genomic_DNA.
DR   RefSeq; WP_011753934.1; NC_008699.1.
DR   STRING; 196162.Noca_0441; -.
DR   EnsemblBacteria; ABL79983; ABL79983; Noca_0441.
DR   KEGG; nca:Noca_0441; -.
DR   eggNOG; ENOG4107RD1; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000236508; -.
DR   KO; K04075; -.
DR   OMA; DPHNADP; -.
DR   OrthoDB; 666797at2; -.
DR   Proteomes; UP000000640; 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; A1SDU8.
DR   SWISS-2DPAGE; A1SDU8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995156}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00437278};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054817};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054814}.
FT   DOMAIN       27    202       ATP_bind_3. {ECO:0000259|Pfam:PF01171}.
FT   DOMAIN      248    315       TilS. {ECO:0000259|Pfam:PF09179}.
FT   NP_BIND      32     37       ATP. {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   COILED      217    244       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   321 AA;  34192 MW;  3B6240071D232D8F CRC64;
     MSLHPAIAAV RLAVRRALAH VDPGRTVVVA CSGGADSLAL LAATVFEGRR AGWRVVGATV
     DHGLQPGSAD HAAHVVRQMA ALGADETVAA TVHVEAAGQG PEAAARQARY AVLDQLAERF
     DADAVLLGHT RDDQAETVLL GLARGSGGRS LAGMRRSFDR FVRPLLDLSR ADTATACQVA
     GIEFWSDPHN EDPAFTRVRV RRSVLPVLED QLGPGVAEAL ARTADQLRAD MDLLDDAAEA
     AYQRLRDLPV DGLLAEPGPI RRRVLRLAAL AAGAPASELF HEHVLAMDAL LTHWHGQKWV
     DLPGKVRCRR ADGRLRLGPA G
//

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