ID   SYR_UREP2               Reviewed;         550 AA.
AC   B1AIR8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=UPA3_0288;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) 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; CP000942; ACA32803.1; -; Genomic_DNA.
DR   RefSeq; WP_006688892.1; NC_010503.1.
DR   AlphaFoldDB; B1AIR8; -.
DR   SMR; B1AIR8; -.
DR   PRIDE; B1AIR8; -.
DR   EnsemblBacteria; ACA32803; ACA32803; UPA3_0288.
DR   GeneID; 29672519; -.
DR   KEGG; upa:UPA3_0288; -.
DR   HOGENOM; CLU_006406_0_1_14; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000002162; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..550
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076236"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   550 AA;  63662 MW;  0400D6105A17A69B CRC64;
     MITQKISEEL NKALAKMGIH DTQETKILVD KTKNIKFGDF YTNIAMILSK KNNKSSLEIA
     KEIANNFEQD LFLEVNLQPP GFLNFKLKAK DHENLLKQIY YEKDRFGQFS KKNITYNIEY
     VSANPTGYLH IAHAANAIYG DILANLLKIY GYDVETEYWI NDAGNQIDKL AMSVLVRYLQ
     LQNINIQLPA DAYHGQEIHL VAQTLYQTYK NQFINVRLNE KYEIDDDIAN QEIKNFAVKY
     LLNEIKNDLA SINTFIDTYT SENWIRNSGR ILEVLSKIKP YTYTLDGALW LKTTTFGDDK
     DRVLIKSDGS YTYFTPDIAY HDYKFNKTNT TKLIDVWGTD HLGYIARLKA AMNALGYDPN
     NLEIVCAQVM KLVKNNQEFK LSKRSGQSLT IKDLVEIIGK DALRWFLGSS SMNSHVIIDV
     DIALSKNNNN PLYYVQYAHA RANQVLNKQV YELDFKTDLL TETRERELLN QLHFYKQTIA
     NAANNREPHR ISNYLYDLAQ IFHNYYANVK INNDNNKVLS AQRYTLVWCV KQVLANGLAI
     MKITPYDQMY