(data stored in SCRATCH zone)

HOGENOM: BACC2_1_PE5349

ID   BACC2_1_PE5349                       STANDARD;      PRT;   556 AA.
AC   BACC2_1_PE5349; B7IR17;
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 2; EC=6.1.1 19;AltName:
DE   Full=Arginine--tRNA ligase 2; (BACC2_1.PE5349).
GN   Name=argS2; OrderedLocusNames=BCG9842_B5465;
OS   BACILLUS CEREUS G9842.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=405531;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACC2_1.PE5349.
CC       Bacillus cereus G9842, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:B7IR17_BACC2
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000247214 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B7IR17; -.
DR   EMBL; CP001186; ACK96541.1; -; Genomic_DNA.
DR   RefSeq; YP_002448901.1; NC_011772.1.
DR   ProteinModelPortal; B7IR17; -.
DR   STRING; B7IR17; -.
DR   EnsemblBacteria; EBBACT00000106009; EBBACP00000101238; EBBACG00000106002.
DR   GeneID; 7183338; -.
DR   GenomeReviews; CP001186_GR; BCG9842_B5465.
DR   KEGG; bcg:BCG9842_B5465; -.
DR   GeneTree; EBGT00050000002259; -.
DR   OMA; FDVYFHE; -.
DR   ProtClustDB; PRK01611; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:HAMAP.
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; BACC2_1.PE5349; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   556 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNSLEQVKGL IKEEIQAAVL KAELATEEQI PNVVLESPKD KTNGDFSTNM AMQLARVAKK
     APRMIAEELV ANFDKAKASI EKIEIAGPGF INFYMDNSYL TDLIPTIVNA GEAYGETNTG
     KGEKVQVEFV SANPTGDLHL GHARGAAVGD TLCNVLAKAG YDVSREYYIN DAGNQIHNLA
     LSVEARYMQA LGLDKEMPED GYHGADIIGI GKRLAEEFGD RYAKADAEES YEFYRSYGLK
     YELAKLQKDL ESFRVKFDVW FSETSLYKNG KIDAALTVLK ERDEIFEEGG ATWFRSMTYG
     DDKNRVLIKN DGSYTYLTPD IAYHRDKLER GFDKLINIWG ADHHGYIPRM KAAIQALGYD
     KETLEVEIIQ MVQLYQNGEK MKMSKRTGKA VTLRELMEEV GVDAMRYFFA MRSGDSHLDF
     DMDLAVSKSN ENPVYYAQYA HARVCSILRQ GEELGLAADG DVNYKLVTSE KEVELLKKLG
     EFPAVVADAA QKRLPHRITS YAFELAAALH SFYNAEKVLN QDNLELSKAR YELMKAVRTT
     LQNALAIVGV SAPEKM
//

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