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SYR_SYNS9
ID   SYR_SYNS9               Reviewed;         590 AA.
AC   Q3AVY5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=Syncc9902_2134;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000097; ABB27092.1; -; Genomic_DNA.
DR   RefSeq; WP_011360874.1; NC_007513.1.
DR   AlphaFoldDB; Q3AVY5; -.
DR   SMR; Q3AVY5; -.
DR   STRING; 316279.Syncc9902_2134; -.
DR   EnsemblBacteria; ABB27092; ABB27092; Syncc9902_2134.
DR   KEGG; sye:Syncc9902_2134; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000002712; 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..590
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242105"
FT   MOTIF           130..140
FT                   /note="'HIGH' region"
SQ   SEQUENCE   590 AA;  64955 MW;  E0DE3A6C56EB8460 CRC64;
     MLSLSQTLDA QLRAAMQRAF PDAEATLDPQ LAAASKPEFG DFQANGALPL AKPLKQPPRQ
     IATAIVDQLS GDEAFNALCL APQIAGPGFI NLTIRPERLA EELAARLGTD RLGVPVVEDV
     APVVVDFSSP NIAKEMHVGH LRSTIIGDSL ARVLEFRGHS VLRLNHVGDW GTQFGMLITH
     LKQVAPETLD TADAVDLGDL VAFYREAKKR FDDDDDFQAT SRDEVVKLQG GDPVSLKAWG
     LLCDQSRREF QKLYDRLDIR LTERGESFYN PYLPAVLDGL KAVDLLVTDD GAQCVFLEGV
     TGKDGNPLPV IVQKRDGGFN YATTDLAAIR FRFASPPTGD AAQRVIYVTD AGQANHFAGV
     FQVAERAGWI PDGARLEHVP FGLVQGEDGK KLKTRAGDTV RLRDLLDEAV ERSEQDLRSR
     LQEEERTESD AFISHVATTV GLAAVKYADL SQNRLTNYQF SFDRMLALQG NTAPYLLYAV
     VRIAGIARKG GDLGVSNAAL QFSEPQEWAL VRELLKFDRV IVEVEDELLP NRLCSYLFEL
     SQVFNRFYDQ VPVLKAEPEA LSSRLALCRH TADTLRCGLA LLGIPTLERM
 
 
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