(data stored in SCRATCH zone)

HOGENOM: AMYMU_1_PE7679

ID   AMYMU_1_PE7679                       STANDARD;      PRT;   553 AA.
AC   AMYMU_1_PE7679; D8HQ81;
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; (AMYMU_1.PE7679).
GN   Name=argS; Synonyms=argS2; OrderedLocusNames=AMED_7797;
OS   AMYCOLATOPSIS MEDITERRANEI U32.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=749927;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AMYMU_1.PE7679.
CC       Amycolatopsis mediterranei U32 chromosome, complete genome.
CC       Missing 5 prime End;
CC   -!- ANNOTATIONS ORIGIN:D8HQ81_AMYMU
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; D8HQ81; -.
DR   EMBL; CP002000; ADJ49505.1; -; Genomic_DNA.
DR   RefSeq; YP_003769907.1; NC_014318.1.
DR   ProteinModelPortal; D8HQ81; -.
DR   GeneID; 9441940; -.
DR   GenomeReviews; CP002000_GR; AMED_7797.
DR   KEGG; amd:AMED_7797; -.
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; AMYMU_1.PE7679; -.
KW   arginyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   553 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTPAALADLV RSSAVQVLAA RGIDDAVLPE QVTIERPRNP DHGDYATNLA LQVAKKAGLK
     PRDFAEALAA AVSADDGVAS AEVAGPGFLN FRLAAAAQGD IVRQVLDAGA AYGRGDALAG
     TRINLEFVSA NPTGPIHLGG TRWAAVGDAL GRVLAAQGAD VTREYYFNDA GAQIDRFVRS
     LIAAAKGEPA PEDGYAGGYI NDIAAEVIKA EPSALSLPEA ERHETFRRIG INLMFSEIKQ
     SLHDFGTDFD VYFHENSLHE SGAVDAAVQQ LKDSGNLYFD EGAWWLKSSE YGDDKDRVVI
     KQDGNPAYIA GDLAYFKDKR NRGFDLCIYM LGADHHGYTA RLKAAAAAFG DDPATVEVLI
     GQMVNLVSDG KPVRMSKRAG TVITMEDLVE AVGVDPARYE LIRYSVDSTL DVDLDLLRKH
     SNDNPVYYVQ YAHARLCTML RGAADLGLKS TEDVDLGQLT LPVEGDLIRT IGEFPETVRR
     AAEMREPHRI ARYLEELAGA LHKFYAVREA RVLPKGDEAA TPANHARVAL CEAARVVLAN
     GLALVGVSAP ERM
//

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