(data stored in SCRATCH zone)

HOGENOM: BACWK_5_PE5035

ID   BACWK_5_PE5035                       STANDARD;      PRT;   556 AA.
AC   BACWK_5_PE5035; A9VSF8;
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; (BACWK_5.PE5035).
GN   Name=argS2; OrderedLocusNames=BcerKBAB4_5158;
OS   BACILLUS WEIHENSTEPHANENSIS KBAB4.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=315730;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACWK_5.PE5035.
CC       Bacillus weihenstephanensis KBAB4, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A9VSF8_BACWK
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; A9VSF8; -.
DR   EMBL; CP000903; ABY46304.1; -; Genomic_DNA.
DR   RefSeq; YP_001647932.1; NC_010184.1.
DR   ProteinModelPortal; A9VSF8; -.
DR   STRING; A9VSF8; -.
DR   EnsemblBacteria; EBBACT00000076924; EBBACP00000074858; EBBACG00000076915.
DR   GeneID; 5845399; -.
DR   GenomeReviews; CP000903_GR; BcerKBAB4_5158.
DR   KEGG; bwe:BcerKBAB4_5158; -.
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; BACWK_5.PE5035; -.
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
     APRMIAEDLV ANFDKAKASI EKIEIAGPGF INFYMDNSYL TDLIPTIVNA GEAYGETNTG
     KGEKVQIEFV SANPTGDLHL GHARGAAVGD TLCNVLAKAG YDVSREYYIN DAGNQIHNLA
     LSVEARYMQA LGLEKEMPED GYHGADIIGI GKRLAEEFGD RYAKADAEES YEFYRSYGLK
     YELAKLQKDL ASFRVNFDVW FSETSLYKNG KIDQALAVLK QRDEIFEEGG ATWFRSMTYG
     DDKNRVLIKN DGSYTYLTPD IAYHRDKLER GFDKLINIWG ADHHGYIPRM KAAIQALGYD
     KETLEVEIIQ MVQLYQNGEK MKMSKRTGKA VTLRELMEEV GVDAMRYFFA MRSGDSHLDF
     DMDLAVSKSN ENPVYYAQYA HARVCSILRQ GEELGLATGG DVNYKLVTSE KEVELLKKLG
     EFPAVVADAA QKRLPHRITS YAFELAAALH SFYNAEKVLN QDNLELSKAR YELMKAVRTT
     LQNALAIVGV SAPEKM
//

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