(data stored in ACNUC7421 zone)

HOGENOM: ECO26_1_PE1009

ID   ECO26_1_PE1009                       STANDARD;      PRT;   466 AA.
AC   ECO26_1_PE1009; C8TM46;
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; (ECO26_1.PE1009).
GN   Name=asnS; OrderedLocusNames=ECO26_1057;
OS   ESCHERICHIA COLI O26:H11 STR. 11368.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=573235;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECO26_1.PE1009.
CC       Escherichia coli O26:H11 str. 11368, complete genome.
CC       1..66570 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:C8TM46_ECO26
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; C8TM46; -.
DR   EMBL; AP010953; BAI24373.1; -; Genomic_DNA.
DR   RefSeq; YP_003228113.1; NC_013361.1.
DR   ProteinModelPortal; C8TM46; -.
DR   SMR; C8TM46; 6-465.
DR   STRING; C8TM46; -.
DR   EnsemblBacteria; EBESCT00000174046; EBESCP00000164506; EBESCG00000170927.
DR   GeneID; 8482037; -.
DR   GenomeReviews; AP010953_GR; ECO26_1057.
DR   KEGG; eoj:ECO26_1057; -.
DR   GeneTree; EBGT00050000009271; -.
DR   ProtClustDB; PRK03932; -.
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; ECO26_1.PE1009; -.
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 QGRVAVDSEV TVRGWVRTRR DSKAGISFLA VYDGSCFDPV QAVINNSLPN
     YNEDVLRLTT GCSVIVTGKV VASPGQGQQF EIQASKVEVA GWVEDPDTYP MAAKRHSIEY
     LREVAHLRPR TNLIGAVARV RHTLAQALHR FFNEQGFFWV STPLITASDT EGAGEMFRVS
     TLDLENLPRN DQGKVDFDKD FFGKESFLTV SGQLNGETYA CALSKIYTFG PTFRAENSNT
     SRHLAEFWML EPEVAFANLN DIAGLAEAML KYVFKAVLEE RADDMKFFAE RVDKDAVSRL
     ERFIEADFAQ VDYTDAVTIL ENCGRKFENP VYWGVDLSSE HERYLAEEHF KAPVVVKNYP
     KDIKAFYMRL NEDGKTVAAM DVLAPGIGEI IGGSQREERL DVLDERMLEM GLNKEDYWWY
     RDLRRYGTVP HSGFGLGFER LIAYVTGVQN VRDVIPFPRT PRNASF
//

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