(data stored in SCRATCH zone)

HOGENOM: BACCN_2_PE3688

ID   BACCN_2_PE3688                       STANDARD;      PRT;   556 AA.
AC   BACCN_2_PE3688; A7GVA6;
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; (BACCN_2.PE3688).
GN   Name=argS2; OrderedLocusNames=Bcer98_3878;
OS   BACILLUS CYTOTOXICUS NVH 391-98.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=315749;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACCN_2.PE3688.
CC       Bacillus cereus subsp. cytotoxis NVH 391-98, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A7GVA6_BACCN
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; A7GVA6; -.
DR   EMBL; CP000764; ABS24064.1; -; Genomic_DNA.
DR   RefSeq; YP_001377059.1; NC_009674.1.
DR   ProteinModelPortal; A7GVA6; -.
DR   STRING; A7GVA6; -.
DR   EnsemblBacteria; EBBACT00000039650; EBBACP00000038701; EBBACG00000039641.
DR   GeneID; 5347434; -.
DR   GenomeReviews; CP000764_GR; Bcer98_3878.
DR   KEGG; bcy:Bcer98_3878; -.
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; BACCN_2.PE3688; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   556 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNSLEQVKEL IKEEIKAAVL KAELATEEQI PNVILETPKD KTHGDFSTNM AMQLARVAKK
     APRMIAEELI TNFNKEKASI EKIEIAGPGF INFHMDNSYL TDLIPTIVKA GEAYGETNTG
     KGEKIQVEFV SANPTGDLHL GHARGAAVGD TLCNVLAKAG YDVSREYYIN DAGNQIHNLA
     LSVEARYMQA LGLEKEMPED GYHGADIMEI GKRLAEEFGD RYVKADEKES YEFYRQYGLK
     YELAKLQKDL DSFRVKFDVW FSETSLYKNG KIDAALAVLK ERNEIFEEGG ATWFRSTAYG
     DDKDRVLIKK DGSYTYLTPD IAYHRDKLER GFDKLINIWG ADHHGYIPRM KAAIQALGYE
     KETLEVEIIQ MVQLYQNGEK VKMSKRTGKA VTLRELMEEV GVDAMRYFFA MRSGDSHLDF
     DMDLAVSKSN ENPVYYAQYA HARVCSILRQ GEELGLHAGG DVNYKLVASE KEIDLLKKLG
     EFPAAVAEAA QKRLPHRITS YAFELAAALH SFYNAEKVLN QDNLELSKAR YELMKAVRIT
     LQNALALVGV SAPEKM
//

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