(data stored in ACNUC7421 zone)

SWISSPROT: SYR_THEFY

ID   SYR_THEFY               Reviewed;         576 AA.
AC   Q47TB0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 96.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   OrderedLocusNames=Tfu_0269;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-
CC         arginyl-tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658,
CC         Rhea:RHEA-COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513,
CC         ChEBI:CHEBI:456215; EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00123}.
DR   EMBL; CP000088; AAZ54307.1; -; Genomic_DNA.
DR   RefSeq; WP_011290716.1; NC_007333.1.
DR   SMR; Q47TB0; -.
DR   STRING; 269800.Tfu_0269; -.
DR   EnsemblBacteria; AAZ54307; AAZ54307; Tfu_0269.
DR   KEGG; tfu:Tfu_0269; -.
DR   eggNOG; ENOG4105C75; Bacteria.
DR   eggNOG; COG0018; LUCA.
DR   HOGENOM; HOG000247212; -.
DR   KO; K01887; -.
DR   OMA; ALCVFFD; -.
DR   OrthoDB; 1146366at2; -.
DR   BioCyc; TFUS269800:G1G4Q-273-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR11956; PTHR11956; 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; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TB0.
DR   SWISS-2DPAGE; Q47TB0.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    576       Arginine--tRNA ligase.
FT                                /FTId=PRO_0000242110.
FT   MOTIF       122    132       "HIGH" region.
SQ   SEQUENCE   576 AA;  63414 MW;  8523BC37722CB1E1 CRC64;
     MADPQTVLAR RVQSALGAAF GPEYRDTDPV IRPSQFADFQ ANVALALAKR LRRSPRDVAT
     AITEHLDISD VCSKVEISGP GFINLTLRDD WIAHQVHDLL TDERLGTPVQ ESQNIPIDYS
     APNVAKEMHV GHLRTTVVGD ALARILEFLG HHVIRQNHIG DWGTPFGMLI EHLLEVGEDS
     AEAAQLKSDP NAFYQAARAK FDSDEDFADR ARRRVVALQS GDAETLRLWR DLIELSKIYF
     NRIYRKLDVT LTDAHLAGES TYNDMLGPVC DELAEKGLAV VSDGALCVFL EGFTGREGKP
     VPLIIRKSDG GYGYATTDLA TIKYRVEQLK ADRIIYVVGA PQSLHLRMVY ETARQAGWLG
     NAEPIHVQIG NVLGSDGKIL RTRSGAPVRL MALLDEAVER ASAVVAQTRP DLDEETRAAI
     ARDVGIGAVK YADLSIAHDT EYVFDFDRML ALNGNTGPYL QYAVARIRSI FRKGGIDPAQ
     VTGPIQVTEP AERALALKLL DFGATVVQVG DTLEPHRLCT YLFDLAQTFT AFYEACPVLK
     ADRDEVRNSR LALTAVTLHT LVKGLDLLGV RAPEQM
//

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