(data stored in SCRATCH zone)

HOGENOM: SALTD_1_PE1001

ID   SALTD_1_PE1001                       STANDARD;      PRT;   466 AA.
AC   SALTD_1_PE1001; C9XDH5;
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=Asparaginyl-tRNA synthetase; EC=6.1.1 22;AltName:
DE   Full=Asparagine--tRNA ligase; (SALTD_1.PE1001).
GN   Name=asnS; OrderedLocusNames=STMMW_10111;
OS   SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. D23580.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella; Salmonella enterica subsp. enterica
OC   serovar Typhimurium.
OX   NCBI_TaxID=568708;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SALTD_1.PE1001.
CC       Salmonella typhimurium (strain D23580) chromosome, complete sequence.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C9XDH5_SALTD
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000226033 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C9XDH5; -.
DR   EMBL; FN424405; CBG24020.1; -; Genomic_DNA.
DR   ProteinModelPortal; C9XDH5; -.
DR   PRIDE; C9XDH5; -.
DR   GenomeReviews; FN424405_GR; STMMW_10111.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 1; -.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004522; Asn-tRNA-synth_IIb.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   TIGRFAMs; TIGR00457; AsnS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   HOGENOMDNA; SALTD_1.PE1001; -.
KW   CBG24020.110037236820036002503210000011;
KW   Asparaginyl-tRNA synthetase ;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   466 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSVVPVADVL QGRVAVDQEV TVRGWVRTRR DSKAGISFLA VYDGSCFDPV QAVINNSLPN
     YNEEVLHLTT GCSVVVTGKV VASPGQGQSF EIQATKVEVA GWVEDPDTYP MAAKRHSIEY
     LREVAHLRPR TNLIGAVARV RHTLAQALHR FFDEQGFFWV STPLITASDT EGAGEMFRVS
     TLDLENLPRN DQGRVDFDKD FFGKESFLTV SGQLNGETYA CALSKIYTFG PTFRAENSNT
     SRHLAEFWML EPEVAFADLE DNARLAEAML KYVFNAVLEE RADDMKFFAE RVDKDAIARL
     ERFVSTDFAQ VDYTDAVAIL ERCGKTFENP VFWGVDLSSE HERYLAEEHF KAPVVVKNYP
     KEIKAFYMRL NEDGKTVAAM DVLAPGIGEI IGGSQREERL DVLDARMAEM GLNKEDYWWY
     RDLRRYGTVP HSGFGLGFER LIAYVTGVQN VRDVIPFPRT PRNASF
//

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