(data stored in SCRATCH zone)

SWISSPROT: A8LE00_FRASN

ID   A8LE00_FRASN            Unreviewed;       608 AA.
AC   A8LE00;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
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=Franean1_0299 {ECO:0000313|EMBL:ABW09765.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09765.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000820; ABW09765.1; -; Genomic_DNA.
DR   RefSeq; WP_012157742.1; NC_009921.1.
DR   STRING; 298653.Franean1_0299; -.
DR   EnsemblBacteria; ABW09765; ABW09765; Franean1_0299.
DR   KEGG; fre:Franean1_0299; -.
DR   eggNOG; ENOG4107RD1; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   eggNOG; COG0634; LUCA.
DR   HOGENOM; HOG000286625; -.
DR   KO; K00760; -.
DR   OMA; RWRGQKP; -.
DR   OrthoDB; 958547at2; -.
DR   BioCyc; FSP298653:G1G9X-297-MONOMER; -.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01992; PP-ATPase; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
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; PF00156; Pribosyltran; 1.
DR   Pfam; PF09179; TilS; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8LE00.
DR   SWISS-2DPAGE; A8LE00.
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:UP000001313};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00437278};
KW   Glycosyltransferase {ECO:0000313|EMBL:ABW09765.1};
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:UP000001313};
KW   Transferase {ECO:0000313|EMBL:ABW09765.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054814}.
FT   DOMAIN       26    197       ATP_bind_3. {ECO:0000259|Pfam:PF01171}.
FT   DOMAIN      270    336       TilS. {ECO:0000259|Pfam:PF09179}.
FT   DOMAIN      436    585       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
FT   NP_BIND      31     36       ATP. {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   COILED      212    239       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   608 AA;  63246 MW;  582C8640AA7A098B CRC64;
     MPAPAVAAVR LAVRDAVADV PPGGLVLVAC SGGADSLALA AALAFVAPRR ALRAGLLTVD
     HGWDDTSRPR AEEVAASGRL LGLSPVEVLA APSPRSEGAA RDSRRAALLA AGERLGAHAV
     LLGHTLDDQA ETVLLRLARG SGARSLSGMP ATDGAIRRPL LRLRRDQTRQ ACQSLGLEFW
     DDPTNADPAF ARARTRSTVL PVLEAELGPG IAEALARTAD LLRADADALE AQAESVYAEL
     AGSAAGTTAP RAPRTPLAAE AEPGPRVEFD VAALAGLTQA LRSRVLRRAA LAAGSSASAL
     RADHIWAVED LVTRWRGQKP VPLPSGVLAR RTGGRITLVG PDAPVRPDTP AGAGHPGRPG
     VVRTPGERGG PTSRAPASGT LTPGTPASGD RGPGDPARNE EDRPVSQAAT AKPDHDGTSI
     PAGGPPRAHP DIDEILVSQD EIAAKIAELA ARVDADYAGR EILLVGVLKG AVMVMADLSR
     ALSVPITMEF MAVSSYGSTT SSSGVVRILK DLDRSIEGRD VLVVEDIIDS GLTLSWLLRN
     LRSRGPASLE VLALFRKPEA ITVDVDVRYV GFDIPSAFVV GYGLDYAEHY RTLPFVGTLT
     PEAIARRA
//

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