ID   SYR_SYNE7               Reviewed;         584 AA.
AC   Q8KPU9; Q31MW2;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   27-MAR-2024, entry version 117.
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=Synpcc7942_1577; ORFNames=sed0009;
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., Gonzalez A.,
RA   Salinas I., McMurtry S., Golden S.S., Youderian P.;
RT   "Synechococcus elongatus PCC7942 cosmid 6C3.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB57607.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY120852; AAM82666.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57607.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039755959.1; NZ_JACJTX010000004.1.
DR   AlphaFoldDB; Q8KPU9; -.
DR   SMR; Q8KPU9; -.
DR   STRING; 1140.Synpcc7942_1577; -.
DR   PaxDb; 1140-Synpcc7942_1577; -.
DR   GeneID; 76400315; -.
DR   KEGG; syf:Synpcc7942_1577; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
DR   OrthoDB; 9805987at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1577-MONOMER; -.
DR   Proteomes; UP000889800; 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; Reference proteome.
FT   CHAIN           1..584
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151625"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
FT   CONFLICT        516
FT                   /note="D -> N (in Ref. 1; AAM82666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        561
FT                   /note="L -> V (in Ref. 1; AAM82666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="A -> G (in Ref. 1; AAM82666)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   584 AA;  65052 MW;  A84B3956A6DF5BBA CRC64;
     MAAPLAQLRD RFQAALAASF GPEWAATDPL LVPATNPKFG DYQSNVAMSL AKQLGQPPRA
     IAETLVQNLN LADLCEPPAI AGPGFINFTL QPSYLVAQLQ QLQTDERLGI QPVSPPQRVI
     VDFSSPNIAK EMHVGHLRST IIGDSIARVL EFQGHEVLRL NHVGDWGTQF GMLIAFLQEQ
     YPQALSQPDA LDISDLVAFY KQAKARFDED PSFQETARQR VVDLQSGEAT ARQAWQLLCD
     QSRREFQKIY DRLDIQLEER GESFYNPYLP AIVEDLRRLG LLVEDQGAQC VFLEGFQNKE
     GQPLPLIVQK SDGGYNYATT DLAALRYRLG QDQAQRIIYV TDSGQANHFA QVFQVAQRAG
     WLPAAAQIEH VPFGLVQGED GKKLKTRAGD TVRLRDLLDE AVDRARTDLT TRIAAEERSE
     TPEFIEAVAQ AVGLGAVKYA DLSQNRNSNY IFSFDKMLAL QGNTAPYLLY AYVRIQGIAR
     KGGIDFAQLD PVAAVLTEPT ERSLAKQVLQ LGEVLDEVAR DLLPNRLCSY LFELSQTFNQ
     FYDRCPILNA EEPQRTSRLL LCDLTARTLK LGLSLLGISV LERM
//