(data stored in SCRATCH zone)

HOGENOM: BACEL1_1_PE4058

ID   BACEL1_1_PE4058                      STANDARD;      PRT;   555 AA.
AC   BACEL1_1_PE4058; E6TY31;
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; (BACEL1_1.PE4058).
GN   Name=argS2; OrderedLocusNames=Bcell_4123;
OS   BACILLUS CELLULOSILYTICUS DSM 2522.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=649639;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACEL1_1.PE4058.
CC       Bacillus cellulosilyticus DSM 2522 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E6TY31_BACCJ
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; E6TY31; -.
DR   EMBL; CP002394; ADU32350.1; -; Genomic_DNA.
DR   RefSeq; YP_004097081.1; NC_014829.1.
DR   ProteinModelPortal; E6TY31; -.
DR   GeneID; 10090723; -.
DR   GenomeReviews; CP002394_GR; Bcell_4123.
DR   KEGG; bco:Bcell_4123; -.
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; BACEL1_1.PE4058; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   555 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQVEQLKET LKSEIIAAVI KAQLATTENI PGVVIESPKE KEHGDYATNM AMQLARIAKK
     APRMIADDIV ANFNKEAASV EKIEIAGPGF INFFMKKDYL SEIVSTVLKQ GNAFGKVNVG
     EGKRLQVEFV SANPTGTLHL GHARGAAVGD SLCNILEKAG YDVAREYYIN DAGNQIENLA
     RSIDARYLQA LGKDVPMPED GYHGQDIIGF AKEIADTYGD RFIDAEEKER LAFFREYGLK
     RELDKLKEDL ADFRVNFDHW YSETSLYTTE KVTDVLTELK NRGETYEEDG AVWFRSTTYG
     DDKDRVLVKS DGSYTYLTPD ISYHKDKFAR GFEELINIWG ADHHGYIPRM KAAIQALGYE
     KEQLSVQIIQ MVNLFENGEK VKMSKRTGKA VTMRDLMEEV GIDATRYFFA MRAADTHLDF
     DMSLAKSQST ENPVYYVQYA HARICSMLRQ ARDLGYEVDP HAQFERLTAE KELDLMKKLG
     EYPEAVADAA KKRAPHRMAN YVYDLAQTLH SFYNAEKVIN EDSELTKARL GLMEAVRATL
     QDALKLVGVE APEKM
//

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