(data stored in SCRATCH zone)

HOGENOM: CHABO1_1_PE166

ID   CHABO1_1_PE166                       STANDARD;      PRT;   562 AA.
AC   CHABO1_1_PE166; Q5L6U4;
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; (CHABO1_1.PE166).
GN   Name=argS; OrderedLocusNames=CAB169;
OS   CHLAMYDOPHILA ABORTUS S26/3.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
OX   NCBI_TaxID=218497;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHABO1_1.PE166.
CC       Chlamydophila abortus S26/3, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:SYR_CHLAB
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; Q5L6U4; -.
DR   EMBL; CR848038; CAH63627.1; -; Genomic_DNA.
DR   RefSeq; YP_219598.1; NC_004552.2.
DR   ProteinModelPortal; Q5L6U4; -.
DR   GeneID; 3337258; -.
DR   GenomeReviews; CR848038_GR; CAB169.
DR   KEGG; cab:CAB169; -.
DR   OMA; YEWANDI; -.
DR   PhylomeDB; Q5L6U4; -.
DR   ProtClustDB; PRK01611; -.
DR   BioCyc; CABO218497:CAB169-MON; -.
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; CHABO1_1.PE166; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   562 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTLLSYLSSL CREAILSAFP QIETISPDIT QSTKELFGHY QCNDAMKLAR TLKMPPRAIA
     ESIVKQISKN NFSSIEIAGA GFINFTFSKE FLNLSLQSYS RDLSSGFRVQ DPKKVVIDFS
     SPNIAKDMHV GHLRSTIIGD CLARIFTFVG HDVLRLNHIG DWGTAFGMLI TYLQEESSED
     IESLEDLTIL YKKAHVRFAE DAEFKKRSQT NVVALQSGDP KARKLWERIC EISERAFQKI
     YNILDIQIEK RGESFYNPFL PEIIEDLEKK NLITVSDEAK CVFHEGFSIP LMVQKRDGGY
     NYATTDLAAM RYRVEQDHAD RIIIVTDMGQ SLHFQLLEAT ALAAGYLPNK DVFSHVGFGL
     VLDSEGKKFK TRSGENIKLQ ELLDTAIDQA VATLKKHRPE MSDAEITERA PVLGMNAIKY
     ADLSSHRVSD YVFSFEKMLR FEGNTAMFIL YGYVRIQGIK RRLGIEKLSL ESAANIQEPS
     EEALALALLR FPEAIDITLK ELCPHFLTDY LYMLTNKFHA FFRDCHIEGS PHQKERLYLC
     ALVEKTLATG MHLLGLQTLD RL
//

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