ID   SYR_PROM9               Reviewed;         604 AA.
AC   Q31CZ4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=PMT9312_0189;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RX   PubMed=16556843; DOI=10.1126/science.1122050;
RA   Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
RA   Delong E.F., Chisholm S.W.;
RT   "Genomic islands and the ecology and evolution of Prochlorococcus.";
RL   Science 311:1768-1770(2006).
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; CP000111; ABB49251.1; -; Genomic_DNA.
DR   RefSeq; WP_011375755.1; NC_007577.1.
DR   AlphaFoldDB; Q31CZ4; -.
DR   SMR; Q31CZ4; -.
DR   STRING; 74546.PMT9312_0189; -.
DR   KEGG; pmi:PMT9312_0189; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000002715; 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..604
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242065"
FT   MOTIF           142..152
FT                   /note="'HIGH' region"
SQ   SEQUENCE   604 AA;  69957 MW;  0709D1B49785AF06 CRC64;
     MLIIFKELTK QFEQSLLDSL EKNDKRGEFD NLRKNLVTQS SKEEFGDYQC NVCLCLSKIY
     KKKPREISED FVYLLNKNKS ISKLCKSLEI AGPGFINIKL KDEVLINEIK SNIQCPRAGI
     PLIKKDLDSG LSNKVIVDFS SPNIAKEMHV GHLRSTIIGD SISRIFELRG YQVLRLNHVG
     DWGTQFGMLI TQLKDLYSND LEEIGKIKIS DLVEFYKASK KRFDNESEFQ KRSREEVVKL
     QSGDSKSIQA WKLLCDQSRK EFDEIYKNLK IKIKERGESF YNPFLKSVIE DLKFKKILIE
     DQGAKCVFLD GMTNKEGKPL PLIVQKKDGG FNYATTDLAA IRYRFNKAPN GDDASRIIYV
     TDHGQANHFA GVFQVAKKAK WIPDKCQVDH VPFGLVQGID GKKLKTREGE TIRLKDLLNE
     AVRRAKEDLL KRLEDEDRYE TEEFIANTSR IIGLGAVKYA DLSQNRITNY QFSFDKMLSL
     NGNTAPYLLY TLVRISGIKR KNDFVYDSED FQYINYEHKS EWKLIRKLLK FDEVIISIEK
     DLMPNRLCNY LFELCQTFNR FYDQVPILKE EKNIKISRLN LCDLTAKTLK LSLELLGIET
     LERM
//