(data stored in ACNUC7421 zone)

HOGENOM: ESCF3_1_PE1005

ID   ESCF3_1_PE1005                       STANDARD;      PRT;   466 AA.
AC   ESCF3_1_PE1005; B7LNU7;
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; (ESCF3_1.PE1005).
GN   Name=asnS; OrderedLocusNames=EFER_1074;
OS   ESCHERICHIA FERGUSONII ATCC 35469.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCF3_1.PE1005.
CC       Escherichia fergusonii ATCC 35469, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:B7LNU7_ESCF3
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; B7LNU7; -.
DR   EMBL; CU928158; CAQ88603.1; -; Genomic_DNA.
DR   RefSeq; YP_002382237.1; NC_011740.1.
DR   STRING; B7LNU7; -.
DR   EnsemblBacteria; EBESCT00000122474; EBESCP00000115338; EBESCG00000122237.
DR   GeneID; 7119693; -.
DR   GenomeReviews; CU928158_GR; EFER_1074.
DR   KEGG; efe:EFER_1074; -.
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; ESCF3_1.PE1005; -.
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 ENCGKKFENP VYWGVDLSSE HERYLAEEHF KAPVVVKNYP
     KDIKAFYMRL NEDGKTVAAM DVLAPGIGEI IGGSQREERL DVLDERMLEM GLNKEDYWWY
     RDLRRYGTVP HSGFGLGFER LIAYVTGVQN VRDVIPFPRT PRNASF
//

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