(data stored in SCRATCH zone)

HOGENOM: ACTSZ_1_PE1078

ID   ACTSZ_1_PE1078                       STANDARD;      PRT;   575 AA.
AC   ACTSZ_1_PE1078; A6VNB3;
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; EC=6.1.1 19;AltName:
DE   Full=Arginine--tRNA ligase; Short=ArgRS; (ACTSZ_1.PE1078).
GN   Name=argS; OrderedLocusNames=Asuc_1094;
OS   ACTINOBACILLUS SUCCINOGENES 130Z.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACTSZ_1.PE1078.
CC       Actinobacillus succinogenes 130Z, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:SYR_ACTSZ
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000247212 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A6VNB3; -.
DR   EMBL; CP000746; ABR74460.1; -; Genomic_DNA.
DR   RefSeq; YP_001344395.1; NC_009655.1.
DR   ProteinModelPortal; A6VNB3; -.
DR   STRING; A6VNB3; -.
DR   GeneID; 5347590; -.
DR   GenomeReviews; CP000746_GR; Asuc_1094.
DR   KEGG; asu:Asuc_1094; -.
DR   eggNOG; COG0018; -.
DR   OMA; YREAKKH; -.
DR   ProtClustDB; PRK01611; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
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; ACTSZ_1.PE1078; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   575 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNIQQLLSEK IRHAMIAAGA QQPAEPAVRQ SGKPQFGDYQ ANGIMGAAKK LGLNPREFAQ
     KVLDNLNLDG IAEKLEIAGP GFINIFLSKN WLVCHADEML SAVNFGIKTA KPQTIVVDYS
     SPNVAKEMHV GHLRSTIIGD AVVRTLEFLG NHVIRANHVG DWGTQFGMLI AYLEKMENEN
     ASAMQLSDLE AFYRAAKEHY DNDEAFAEKA RNYVVKLQSG DEYCRIMWKK LVDITMRHNQ
     ENYDRLNVTL TEKDVMGESL YNPMLPEIVA DLKKQGLAVE DDGALVVYLD EFKNKDGDPM
     GVIVQKKDGG YLYTTTDIAA AKYRCHKLHA DRVLVFSDSR QSQHMQQAWL ITRKAGYVPD
     SFSLEHPFFG MMLGKDGKPF KTRTGGTVKL KDLLDEAVER ADKLIAERNP DLTAEEKAAV
     VEAVAIGSVK YSDLSKNRTT DYVFDWDNML TFEGNTAPYM QYAYTRIRSI FARAGIEPNS
     LNDDIVLTDD KERVLVIKLL QFEEALNGVA KDGMPHILCQ YLYELAGMFS AFYEACPILN
     AERPIKNSRL KLAALAAKTL KQGLDLLGIK TVEKM
//

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