(data stored in ACNUC7421 zone)

HOGENOM: SPITD_1_PE1011

ID   SPITD_1_PE1011                       STANDARD;      PRT;   472 AA.
AC   SPITD_1_PE1011; E0RSK0;
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; (SPITD_1.PE1011).
GN   Name=tilS; OrderedLocusNames=STHERM_c10420;
OS   SPIROCHAETA THERMOPHILA DSM 6192.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=665571;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SPITD_1.PE1011.
CC       Spirochaeta thermophila DSM 6192 chromosome, complete genome.
CC       nt) ;
CC   -!- ANNOTATIONS ORIGIN:E0RSK0_SPITD
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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC   -!- GENE_FAMILY: HBG000000000 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E0RSK0; -.
DR   EMBL; CP001698; ADN01987.1; -; Genomic_DNA.
DR   RefSeq; YP_003874260.1; NC_014484.1.
DR   GeneID; 9756296; -.
DR   GenomeReviews; CP001698_GR; STHERM_c10420.
DR   KEGG; sta:STHERM_c10420; -.
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:HAMAP.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:HAMAP.
DR   HAMAP; MF_01161; tRNA_Ile__lys_synt; 1; -.
DR   InterPro; IPR012094; Lysidine-tRNA-synth.
DR   InterPro; IPR012795; Lysidine-tRNA-synth_N.
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   PANTHER; PTHR11807:SF2; ATPase_MesJ_YaeO; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   TIGRFAMs; TIGR02432; Lysidine_TilS_N; 1.
DR   HOGENOMDNA; SPITD_1.PE1011; -.
KW   tRNA(Ile)-lysidine synthase;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   tRNA processing.
SQ   SEQUENCE   472 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLEKVYTFFK GFDHVEGAVV LVACSGGPDS TALLHSLFLL RQRLNLTLKV VYLDHGIRPR
     SERDQEYRFV MSLAETRDLP SHIKRLPEGW ILHRAKASKK SVEEVAREER YAFFEELLSK
     GEGDYVALGH TRDDQVETVV FRFLRGSDPL ALRGMSPVRD RYLRPLLSCS RSEVLSFLQE
     QGLSYLEDSS NEKDAYDRNF LRIHVLPVLE KRFPGWTKAV VALSEKAELY HRYLERRDPV
     GGFPIEETPS GLRVPFHLVS RADPLERYLL FYRLYQVFMS REGTSESEEL PFWHIRPYVW
     HPESLWDGIV VGRGVMMRRE GEYLVVRSHV VLHGENGYFV VIEKEGEFRL TDELRMEVRC
     GRHIPFEKGR PGANEMVLPV GTYVCRSRKA GDAVARGSLR RSVHKVFQMW NLPPHLRCSV
     PVLEAPGKGI VAILGGWAGY EDIFADPNPI PFKGDEDVLY IRLHHVGRSI ER
//

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