(data stored in ACNUC7421 zone)

HOGENOM: STRPS_1_PE10

ID   STRPS_1_PE10                         STANDARD;      PRT;   425 AA.
AC   STRPS_1_PE10; B2IQZ8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=tRNA(Ile)-lysidine synthase; EC=6.3.4 -;AltName:
DE   Full=tRNA(Ile)-2-lysyl-cytidine synthase;AltName: Full=tRNA(Ile)-lysidine
DE   synthetase; (STRPS_1.PE10).
GN   Name=tilS; OrderedLocusNames=SPCG_0010;
OS   STREPTOCOCCUS PNEUMONIAE CGSP14.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
OX   NCBI_TaxID=516950;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STRPS_1.PE10.
CC       Streptococcus pneumoniae CGSP14, complete genome.
CC       chromosome 1, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:TILS_STRPS
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC   -!- GENE_FAMILY: HOG000235102 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B2IQZ8; -.
DR   EMBL; CP001033; ACB89262.1; -; Genomic_DNA.
DR   RefSeq; YP_001834727.1; NC_010582.1.
DR   ProteinModelPortal; B2IQZ8; -.
DR   STRING; B2IQZ8; -.
DR   EnsemblBacteria; EBSTRT00000018142; EBSTRP00000017456; EBSTRG00000018142.
DR   GeneID; 6217938; -.
DR   GenomeReviews; CP001033_GR; SPCG_0010.
DR   KEGG; spw:SPCG_0010; -.
DR   GeneTree; EBGT00050000027463; -.
DR   OMA; HQVIPAF; -.
DR   ProtClustDB; CLSK876678; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   HAMAP; MF_01161; tRNA(Ile)-lys_synt; 1; -.
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   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   SUPFAM; SSF56037; B3_4; 1.
DR   TIGRFAMs; TIGR02433; Lysidine_TilS_C; 1.
DR   TIGRFAMs; TIGR02432; Lysidine_TilS_N; 1.
DR   HOGENOMDNA; STRPS_1.PE10; -.
KW   mesJ/ycf62 family protein;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   tRNA processing.
SQ   SEQUENCE   425 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MREQDFLNHF LKKGYFKKHA KAVLALSGGL DSMFLFKVLS TYQKELEIEL ILAHVNHKQR
     IESDWEEKEL RKLAAEAELP IYISNFSGEF SEARARNFRY DFFQEVMKKT GATALVTAHH
     ADDQVETILM RLIRGTRLRY LSGIKEKQVV GEIEIIRPFL HFQKKDFPSI FHFEDTSNQE
     NHYFRNRIRN SYLPELEKEN PRFRDAILGI GNEILDYDLA IAELSNNIDV ENLQQLFSYS
     ESTQRVLLQT YLNRFPDLNL TKAQFAEVQQ ILKSKSQYRH PIKNGYELIK EYQQFQICKI
     SPQADEKEDE LVLHYQNQVA YQGYLFSFGL PLEGELIQQI PVSRETSIHI RHRKTGDVLI
     QNGHRKKLRR LFIDLKIPME KRNSALIIEQ FGEIVSILGI ATNNLSKKTK NDIMNTVLYI
     EKIDR
//

If you have problems or comments...

PBIL Back to PBIL home page