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SYR_NOSS1
ID   SYR_NOSS1               Reviewed;         588 AA.
AC   Q8YQU9;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=all3717;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75416.1; -; Genomic_DNA.
DR   PIR; AF2270; AF2270.
DR   RefSeq; WP_010997860.1; NZ_RSCN01000007.1.
DR   AlphaFoldDB; Q8YQU9; -.
DR   SMR; Q8YQU9; -.
DR   STRING; 103690.17132851; -.
DR   EnsemblBacteria; BAB75416; BAB75416; BAB75416.
DR   KEGG; ana:all3717; -.
DR   eggNOG; COG0018; Bacteria.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000002483; 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..588
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151523"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
SQ   SEQUENCE   588 AA;  65815 MW;  1B778901CB6DF67E CRC64;
     MNATQEQLKI KLEQALVAAF GDEYAGVDPI LVSASNPKFG DYQANVALSL SKKLGQQPRA
     IASAIVEKLD VSEICEKPEI AGPGFINLKL KTAYLEAQLN TIQADTRLGV PTAKHPQREI
     VDFSSPNIAK EMHVGHLRST IIGDSIARIL EFRGHDVLRL NHVGDWGTQF GMLITYLREV
     SPEALTTANA LDIGDLVSFY RQAKQRFDAD EAFQETARQE VVRLQAGAAD TLHAWKLLCE
     QSRQEFQVIY DLLDVKLTER GESFYNPLLP TVVENLEKSG LLVENQGAKC VFLDGFTNRE
     GEPLPLIVQK SDGGYNYATT DLAALRYRIQ KDEAKRIIYI TDAGQANHFA QFFQVARKAG
     WIPDDVELVH VPFGLVLGED GKKFKTRSGD TVRLRDLLDE AISRAHADVE VRLKAEEREE
     TAEFIDKVAE VVGISAVKYA DLSQNRTSNY IFSYDKMLDL KGNTAPYMLY AYARIQGISR
     KGEINFADLG DNAKVILQHE TEFALAKYLL QLGEVISTVE EDLSPNRLCE YLYELSKRFN
     AFYDRNQGVQ VLSAEEPLRT SRLVLCDLTA RTLKLGLSLL GIQVLERM
 
 
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