ID   SYR_TRIV2               Reviewed;         588 AA.
AC   Q3M769;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=Ava_3561;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA23167.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M769; -.
DR   SMR; Q3M769; -.
DR   STRING; 240292.Ava_3561; -.
DR   KEGG; ava:Ava_3561; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
DR   Proteomes; UP000002533; 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; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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.
FT   CHAIN           1..588
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000241974"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
SQ   SEQUENCE   588 AA;  65554 MW;  5CB9FB06D47521AD CRC64;
     MNATQEQLKV KLEQALIAAF GDEYAGVDPI LVTASNPKFG DYQANVALSL SKKLGQPPRA
     IASAIVEKLD VSEICETPEI AGPGFINLKL KTAYLEAQLN AIQADSRLGV PTAKHPQREI
     VDFSSPNIAK EMHVGHLRST IIGDSIARIL EFRGHDVLRL NHVGDWGTQF GMLITYLREV
     SPEALTTANA LDIGDLVSFY RQAKQRFDAD EAFQETARQE VVRLQAGATD TLHAWKLLCE
     QSRQEFQVIY DLLDVKLTER GESFYNPLLP TVVEGLEASG LLVENQGAKC VFLDGFTNRE
     GEPLPLIVQK SDGGYNYATT DLAALRYRIQ KDEAKRIVYV TDAGQANHFA QFFQVARKAG
     WIPNDVELVH VPFGLVLGED GKKFKTRSGD TVRLRDLLDE AVSRAHADLE ERLKAEEREE
     TPEFIDKVAE VVGISAVKYA DLSQNRTSNY IFSYDKMLDL KGNTAPYMLY AYARIQGISR
     KGGINFADLG DNAKVILQHD TEFALAKYLL QLGEVISTVE ADLLPNRLCE YLYELSKKFN
     TFYDRNQGVQ VLSAEEPLRT SRLVLCDLTA RTLKLGLSLL GIQVLERM
//