ID   SYR_MICAN               Reviewed;         585 AA.
AC   B0JLI8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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}; OrderedLocusNames=MAE_31900;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-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 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR   EMBL; AP009552; BAG03012.1; -; Genomic_DNA.
DR   RefSeq; WP_012266140.1; NC_010296.1.
DR   AlphaFoldDB; B0JLI8; -.
DR   SMR; B0JLI8; -.
DR   STRING; 449447.MAE_31900; -.
DR   PaxDb; B0JLI8; -.
DR   EnsemblBacteria; BAG03012; BAG03012; MAE_31900.
DR   KEGG; mar:MAE_31900; -.
DR   PATRIC; fig|449447.4.peg.2891; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   BioCyc; MAER449447:MAE_RS13815-MON; -.
DR   Proteomes; UP000001510; 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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..585
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076221"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
SQ   SEQUENCE   585 AA;  65637 MW;  D38D6794AE298A9C CRC64;
     MTAIIQQIKE RFSQSLVKSF GENFADTDPL IVAASNPRFG DYQCNISLSL AKELKQKPRE
     VAATLLKNLE IDDLCQTPEI AGPGFINLTL KPSYLETQLK DLITDNRLGV ATANPSQKII
     VDFSSPNIAK EMHVGHLRST IIGDCIARIL EFRHHQVIRL NHVGDWGTQF GMLITYLQEA
     YPSALTQADA LDLGDLVSFY KKAKIRFDED ENFKETARQA VVKLQSGDPQ SRQAWQLLCQ
     QSRREFQKIY DILDIKLTER GESFYNPYLE AVIRELDQQG LLTEDNGALC VFLDGFTNKE
     GEPLPLIVKK SDGGYNYATT DLAAICYRVR EDKAERIIYV TDAGQANHFA QVFQVAKKAG
     FLPDNVAVVH VAFGLVLGED GKKLKTRSGE TVKLQELLDQ AIACSLADLE KRLASEEREE
     TGDFIAKTAE TVGLSAVKYA DLSQNRHSNY VFSYDKMLNL QGNTAPYMLY AYARVQSISR
     EGGINFQDLS ANSSLILKDE SELILAKQLL QLPEVISAVE EDLLPNRLCD YLYELSKKYN
     RFYENCPVLK AAEPIKTSRL FLCDLTARTL KLGLSLLGIP VLERM