ID   SYR_PORG3               Reviewed;         597 AA.
AC   B2RHN9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=PGN_0365;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009380; BAG32884.1; -; Genomic_DNA.
DR   RefSeq; WP_012457453.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RHN9; -.
DR   SMR; B2RHN9; -.
DR   STRING; 431947.PGN_0365; -.
DR   EnsemblBacteria; BAG32884; BAG32884; PGN_0365.
DR   GeneID; 29255605; -.
DR   KEGG; pgn:PGN_0365; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_10; -.
DR   OMA; NKPLHLG; -.
DR   BioCyc; PGIN431947:G1G2V-401-MON; -.
DR   Proteomes; UP000008842; 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   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.
FT   CHAIN           1..597
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095390"
FT   MOTIF           125..135
FT                   /note="'HIGH' region"
SQ   SEQUENCE   597 AA;  67522 MW;  6E9378412B9D88DC CRC64;
     MSILQKLENS AAAAVKALYG TDPMEGQIQL QKTKREFKGH LTLVVFPFVK MSRKSPEATA
     TEIGEWLLAN ESAVSAIEVV KGFLNLTIAP RVWLELLNEI RADINFGHKV ATEDSPLVMV
     EYSSPNTNKP LHLGHVRNNL LGYSLSEIMK ANGYRVVKTN IVNDRGIHIC KSMLAWQKWG
     DGVTPEKAGK KGDHLIGDFY VLFDKHYKAE LNSLMAEGKS KEEAEAASTL MAEAREMLRL
     WEAGDEKVVD LWRTMNQWVY DGFEATYKMM GVDFDKIYYE SETYLVGKEE VLRGLEEGLF
     VKHSDGSVWA DLTKDGLDEK LLLRADGTSV YMTQDIGTAK MRFNDYPINR MIYVVGNEQN
     YHFQVLSILL DRLGFEFGKG LVHFSYGMVE LPEGKMKSRE GTVVDADDLM DEMIRTAAEI
     AAEAGKAAEK DEEESREVAR IVGLGSLKYF ILKVDPRKNM TFNPKESIDF NGNTGSFVQY
     TYARIRSLMR RAEAAGYDIP SQLPTDLPLS EKEEALIQKV SEYAEVVSEA GRSYSPALIA
     NYIYDLVKEY NQFYHDFSVL KEEDERIRAF RLALSEVVAL TMRKGFALLG IEMPERM