(data stored in SCRATCH zone)

HOGENOM: CHLTD_1_PE455

ID   CHLTD_1_PE455                        STANDARD;      PRT;   563 AA.
AC   CHLTD_1_PE455; D7DDS7;
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; (CHLTD_1.PE455).
GN   Name=argS; OrderedLocusNames=CTDEC_0454;
OS   CHLAMYDIA TRACHOMATIS D-EC.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=759363;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLTD_1.PE455.
CC       Chlamydia trachomatis (serovar D, strain D-EC) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D7DDS7_CHLTD
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: HOG000247212 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D7DDS7; -.
DR   EMBL; CP002052; ADI51131.1; -; Genomic_DNA.
DR   ProteinModelPortal; D7DDS7; -.
DR   GenomeReviews; CP002052_GR; CTDEC_0454.
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; CHLTD_1.PE455; -.
KW   ADI51131.100024376fold_1320000031;
KW   Arginyl-tRNA synthetase ;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   563 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTTLLSFLTS LCSAAIHQAF PELEELTLDI TPSTKEHFGH YQCNDAMKLA RVLHKSPRAI
     AESIVAHIPP TPFSSIEIAG AGFINFTFSK EFLASQLQTF SKELANGFRA ASPQKVIIDF
     SSPNIAKDMH VGHLRSTIIG DCLARCFSFV GHDVLRLNHI GDWGTAFGML ITYLQETSQE
     AIHQLEDLTA LYKKAHARFA EDSEFKKRSQ HNVVALQSGD AQALALWKQI CSVSEKSFQT
     IYSILDVELH TRGESFYNPF LAEVVADLES KNLVTLSDGA KCVFHEAFSI PLMIQKSDGG
     YNYATTDVAA MRYRIQQDQA DRILIVTDSG QSLHFQLLEA TCLAAGYLPS KGIFSHVGFG
     LVLDTQGRKF KTRSGENIKL RELLDTAVEK AKESLKAHRP DISEEELAYQ GPILGINAIK
     YADLSSHRIN DYVFSFEKML RFEGNTAMSL LYAYVRIQGI KRRMGLESPP QEGPLAVHEP
     AEEALALTLL RFPEILDLTL RELCPHFLTD YLYALTNKFN AFFRDCHIEG SDSQQERLYL
     CGLTERTLST GMHLLGLKTL NHL
//

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