ID F0RN40_DEIPM Unreviewed; 529 AA.
AC F0RN40;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 01-MAY-2013, entry version 16.
DE RecName: Full=tRNA(Ile)-lysidine synthase;
DE EC=6.3.4.19;
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase;
DE AltName: Full=tRNA(Ile)-lysidine synthetase;
GN Name=tilS; OrderedLocusNames=Deipr_1026;
OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 /
OS NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC Deinococcaceae; Deinococcus.
OX NCBI_TaxID=693977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT 20540.";
RL Submitted (FEB-2011) 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: (tRNA(Ile2))-cytidine(34) + L-lysine + ATP =
CC (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H(2)O.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC motif, predicted to be a P-loop motif involved in ATP binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP002536; ADY26182.1; -; Genomic_DNA.
DR RefSeq; YP_004255799.1; NC_015161.1.
DR EnsemblBacteria; ADY26182; ADY26182; Deipr_1026.
DR GeneID; 10256505; -.
DR KEGG; dpt:Deipr_1026; -.
DR PATRIC; 46929842; VBIDeiPro159979_1018.
DR KO; K04075; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:HAMAP.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01161; tRNA_Ile__lys_synt; 1; -.
DR InterPro; IPR002125; CMP_dCMP_Zn-bd.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR012094; Lysidine-tRNA-synth.
DR InterPro; IPR012796; Lysidine-tRNA-synth_C.
DR InterPro; IPR012795; Lysidine-tRNA-synth_N.
DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; tRNA-lysidine/thiocyt_synth.
DR PANTHER; PTHR11807:SF2; PTHR11807:SF2; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF11734; TilS_C; 1.
DR SMART; SM00977; TilS_C; 1.
DR SUPFAM; SSF56037; B3_4; 1.
DR SUPFAM; SSF53927; Cytidine_deaminase-like; 1.
DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW tRNA processing.
FT NP_BIND 22 27 ATP (By similarity).
SQ SEQUENCE 529 AA; 56214 MW; FF94E48310DC7037 CRC64;
MLDALTAALR PYRARQVVVG VSGGADSVAL LRALLAAGAE PLVAHFDHRL RPDSAEDAAW
VEALAGRLGV PYVGGGADVG RVAQVRGWNL EDAARRLRYS FLTRTAKDAG IDTVLTAHTR
RDQAETVLMR LLRGEAVLSG IAPRWGGVER PLLGVAREEL EAYLRALGQD WREDSTNADT
ALTRAWLRLE VLPLLRSRFP AAEEALSGLA GRAAEDEAVL SGLAAAIGPH TPLVGQPPAV
LRRWLRAELD RAGLAVRAGQ LSALAGALAA GETRHLTLPH GQPASVTGGR LVLPGTRPDW
AAPDFAFPPD WQLRTPQPGD RIRLSGGTRR LSDVLAEARV PRAWRPQVPL LASAQGVQWV
GLTPPVWAAG ARERTGWHDP LWEGMEAALT QARAAAAVQE VPVGAAVLDP AGAVVGLGRN
RSRERGDMTR HAELEALRQA ASALGTPYLS GCTLAVTLEP CPMCLGAALE ARVGRIVYGA
ANPRAGALGG VHDLLGHRWG VRPQVQGGYR AGECAGLLKK AFAEFRRQD
//
