(data stored in SCRATCH zone)

HOGENOM: ECOK1_1_PE1718

ID   ECOK1_1_PE1718                       STANDARD;      PRT;   577 AA.
AC   ECOK1_1_PE1718; A1AC37;
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=Arginyl-tRNA synthetase; EC=6.1.1 19;AltName:
DE   Full=Arginine--tRNA ligase; Short=ArgRS; (ECOK1_1.PE1718).
GN   Name=argS; OrderedLocusNames=Ecok1_17330; ORFNames=APECO1_926;
OS   ESCHERICHIA COLI APEC O1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOK1_1.PE1718.
CC       Escherichia coli APEC O1, complete genome.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:SYR_ECOK1
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000247212 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A1AC37; -.
DR   EMBL; CP000468; ABJ01227.1; -; Genomic_DNA.
DR   RefSeq; YP_852941.1; NC_008563.1.
DR   ProteinModelPortal; A1AC37; -.
DR   SMR; A1AC37; 1-577.
DR   STRING; A1AC37; -.
DR   EnsemblBacteria; EBESCT00000036480; EBESCP00000034997; EBESCG00000035530.
DR   GeneID; 4495751; -.
DR   GenomeReviews; CP000468_GR; Ecok1_17330.
DR   KEGG; ecv:APECO1_926; -.
DR   eggNOG; COG0018; -.
DR   GeneTree; EBGT00050000011125; -.
DR   OMA; YREAKKH; -.
DR   ProtClustDB; PRK01611; -.
DR   BioCyc; ECOL405955:APECO1_926-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1; -.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-synth_Ia.
DR   InterPro; IPR015945; Arg-tRNA-synth_Ia_core.
DR   InterPro; IPR005148; Arg-tRNA-synth_Ia_N.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   Gene3D; G3DSA:3.30.1360.70; Arg-tRNA-synth_Ic_N; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11956; Arg_tRNA-synt_1c; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF55190; Arg-tRNA-synth_Ic_N; 1.
DR   SUPFAM; SSF47323; tRNAsyn_1a_bind; 1.
DR   TIGRFAMs; TIGR00456; ArgS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   HOGENOMDNA; ECOK1_1.PE1718; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   577 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNIQALLSEK VRQAMIAAGA PADCEPQVRQ SAKVQFGNYQ ANGMMAVAKK LGMAPRQLAE
     QVLTHLDLNG IASKVEIAGP GFINIFLDPA FLAEHVQQAL ASDRLGVAMP EKQTIVVDYS
     APNVAKEMHV GHLRSTIIGD AAVRTLEFLG HKVIRANHVG DWGTQFGMLI AWLEKQQQEN
     AGEMELADLE GFYRDAKKHY DEDEEFAERA RNYVVKLQSG DEYFREMWRK LVDITMTQNQ
     ITYDRLNVTL TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EFKNKEGEPM
     GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWA IVRKAGYVPE
     SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER ARRLVAEKNP DMPADELEKL
     ANAVGIGAVK YADLSKNRTT DYIFDWDNML AFEGNTAPYM QYAYTRVLSV FRKAEIDEEQ
     LAAAPVIIRE DREAQLAARL LQFEETLTVV AREGTPHVMC AYLYDLAGLF SGFYEHCPIL
     SAENEEVRNS RLKLAQLTAK TLKLGLDTLG IETVERM
//

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