ID   SYR_PYRAE               Reviewed;         630 AA.
AC   Q8ZTA8;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 118.
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=PAE3343;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC   IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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   -!- 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; AE009441; AAL64855.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZTA8; -.
DR   SMR; Q8ZTA8; -.
DR   STRING; 178306.PAE3343; -.
DR   EnsemblBacteria; AAL64855; AAL64855; PAE3343.
DR   KEGG; pai:PAE3343; -.
DR   PATRIC; fig|178306.9.peg.2519; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   InParanoid; Q8ZTA8; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..630
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151651"
FT   MOTIF           120..130
FT                   /note="'HIGH' region"
SQ   SEQUENCE   630 AA;  71667 MW;  40A1D80199267641 CRC64;
     MDPLRQPREE FVKVLGEVSR ELGLPEVPEV ERTRRYGFFS ARFHKYKVDH SRLAEVVNLI
     KNKRFEFLSS LSVDGLYLNA DLNVSKVAEL VFEAVVKMGR KYGFTEECVT GSYLVEHTSA
     NPVHPLHIGH GRNAILGDSL ARLLKFCGNK VETHFYVDDC GVQVMYAAMG YNAVKDEVKK
     RIEKSKPDVV IGHVYSATNA VAEIGRLKKE LEKAQDDERK REILREIDEW VAVLKRLMDS
     EGDIISKIAE ELGRRDLLNE AVELNRRYES GDPEAKGVVR EVVDLVLKGQ RETLARLGVE
     IDKWDYESEL TVWSSEAMRI VSELQKRWPQ YIEIKGGAVV FRADKFVQDY NLWDVLDLPR
     FIPPVTLTRS DGTTLYVTRD VAYALWQARQ GFDKVIRVIS TEQTHEQAHV RIILYALGYV
     DEAKKIVHYA YEMVNLPGMK MSARRGQYIS LDEILDEAAE RSASLVKEKN PEVSGVIAER
     VGVGSVRYAF LTTSPRKPIE FKWDVVLNLR QNSGTFLQYT YVRAYSILEK AGEIGNVPVP
     ENMLAEEREL VLKIAEWPSV VKEAAKSLRP DYVAEYLDGL ALVFNSYYEK APVLKAEESV
     RGFRIAIVNA VKTVLEAGFY ILGIPTLTKM
//