(data stored in SCRATCH zone)

SWISSPROT: A5GQ16_SYNR3

ID   A5GQ16_SYNR3            Unreviewed;       337 AA.
AC   A5GQ16;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161};
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   ECO:0000313|EMBL:CAK26975.1};
GN   OrderedLocusNames=SynRCC307_0072 {ECO:0000313|EMBL:CAK26975.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK26975.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK26975.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) 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   -!- 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; CT978603; CAK26975.1; -; Genomic_DNA.
DR   RefSeq; WP_011934490.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0072; -.
DR   EnsemblBacteria; CAK26975; CAK26975; SynRCC307_0072.
DR   KEGG; syr:SynRCC307_0072; -.
DR   eggNOG; ENOG4107UAN; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000233244; -.
DR   KO; K04075; -.
DR   OMA; DPHNADP; -.
DR   OrthoDB; 666797at2; -.
DR   BioCyc; SSP316278:G1GJL-72-MONOMER; -.
DR   Proteomes; UP000001115; 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   PANTHER; PTHR43033:SF1; PTHR43033:SF1; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQ16.
DR   SWISS-2DPAGE; A5GQ16.
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:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054817, ECO:0000313|EMBL:CAK26975.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054814}.
FT   DOMAIN       36    211       ATP_bind_3. {ECO:0000259|Pfam:PF01171}.
FT   NP_BIND      41     46       ATP. {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   COILED      229    256       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   337 AA;  37961 MW;  FF27F8A02C20778D CRC64;
     MRTILPSGKQ PWSRWHHRLH QLLLDDPSLL PQGSGLLIAI SGGQDSLALT RLLLDLREQH
     HWQLQLWHGN HNWRQDAAAN AQHLQQVAAQ WGLPLTVDCA EPAPKSEAAA RQWRYERLQR
     QAETSSCPLV LTGHTATDRA ETLLFNLIRG ADLTGLSSLR QTRPLGAGIT VVRPLLAFSR
     ADTQACCEQL GLLVWHDITN ADRQFSRNRL RLDVIPELEA LNPGATQHLA RAAQLLEELE
     GQHSALEALA LEAIRSEPGR ADLNRQRWQE QPIKLQKRLL HRWVQQTSQQ QLSAALTTEI
     WRQLQKPGRR PPIALSHGWQ LQAEACMLKL IPPAASD
//

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