(data stored in SCRATCH zone)

SWISSPROT: A4F6R8_SACEN

ID   A4F6R8_SACEN            Unreviewed;       330 AA.
AC   A4F6R8;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=SACE_0394 {ECO:0000313|EMBL:CAL99742.1};
GN   ORFNames=A8924_0790 {ECO:0000313|EMBL:PFG93545.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99742.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99742.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99742.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93545.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93545.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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: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; AM420293; CAL99742.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93545.1; -; Genomic_DNA.
DR   RefSeq; WP_009946441.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0394; -.
DR   EnsemblBacteria; CAL99742; CAL99742; SACE_0394.
DR   KEGG; sen:SACE_0394; -.
DR   eggNOG; ENOG4107RD1; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000236508; -.
DR   KO; K04075; -.
DR   OMA; DPHNADP; -.
DR   OrthoDB; 666797at2; -.
DR   BioCyc; SERY405948:SACE_RS01935-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F6R8.
DR   SWISS-2DPAGE; A4F6R8.
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:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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, ECO:0000313|EMBL:CAL99742.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054814}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    330       tRNA(Ile)-lysidine synthase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011934033.
FT   DOMAIN       32    204       ATP_bind_3. {ECO:0000259|Pfam:PF01171}.
FT   DOMAIN      253    318       TilS. {ECO:0000259|Pfam:PF09179}.
FT   NP_BIND      37     42       ATP. {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   COILED      226    246       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   330 AA;  34585 MW;  51EC946917443D53 CRC64;
     MPPTAAVTAT RAAVRRLLGS AEASPSAPLG AVAVACSGGA DSLALAAATT HVARRRDIAV
     HGLVVDHGLQ EGSADVASRA AEQLEELGCD VVRVLPVEIG REGGPEAAAR RARYAALDAA
     RPAGAPVLLG HTRDDQAETV LLGLGRGSGA RSIAGMRPVD LPWLRPFLDV TRDTTLAACE
     ALGLRPWQDP HNSDAKFTRV RLRAEVLPLL EEVLQGGVAS ALARTAVQLR EDADALDEVA
     ADVRKRVEDG DALDAAALSA GPPAVRRRVL RGWLLDQGVR EVSDAHLRAA DALVGHWKGQ
     GPHALPGGFV LRRTHGTLRV EVAVKQPPDY
//

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