(data stored in SCRATCH zone)

HOGENOM: BACAH_2_PE4617

ID   BACAH_2_PE4617                       STANDARD;      PRT;   556 AA.
AC   BACAH_2_PE4617; A0RLE6;
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; (BACAH_2.PE4617).
GN   Name=argS; Synonyms=argS2; OrderedLocusNames=BALH_4860;
OS   BACILLUS THURINGIENSIS STR. AL HAKAM.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=412694;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACAH_2.PE4617.
CC       Bacillus thuringiensis str. Al Hakam chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:A0RLE6_BACAH
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; A0RLE6; -.
DR   EMBL; CP000485; ABK88039.1; -; Genomic_DNA.
DR   RefSeq; YP_897546.1; NC_008600.1.
DR   ProteinModelPortal; A0RLE6; -.
DR   STRING; A0RLE6; -.
DR   EnsemblBacteria; EBBACT00000067557; EBBACP00000065794; EBBACG00000067548.
DR   GeneID; 4542202; -.
DR   GenomeReviews; CP000485_GR; BALH_4860.
DR   KEGG; btl:BALH_4860; -.
DR   NMPDR; fig|412694.5.peg.4673; -.
DR   eggNOG; COG0018; -.
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; BACAH_2.PE4617; -.
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 TLCNLLAKAG YDVSREYYIN DAGNQIHNLA
     LSVKARYMQA LGLEKEMPED GYHGADIIAI GKRLAEEFGD RYAKADEKES YEFYREYGLK
     YELAKLQKDL ESFRVKFDVW FSETSLYKNG KIDQALAVLK ERDEIFEEDG ATWFRSMTYG
     DDKNRVLIKN DGSYTYLTPD IAYHRDKLER GFDKLINIWG ADHHGYIPRM KAAIQALGYD
     KETLEVEIIQ MVQLYQNGEK MKMSKRTGKA VTLRELMEEV GVDAMRYFFA MRSGDSHLDF
     DMDLAVSKSN ENPVYYAQYA HARVCSILRQ GEELGLATDG DVNYKLVTSE KEVELLKKLG
     EFPAVVADAA QKRLPHRITN YAFELAAALH SFYNAEKVLN QDNVELSKAR YELMKAVRTT
     LQNALAIVGV SAPEKM
//

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