ID   SYR_SACS2               Reviewed;         625 AA.
AC   Q97ZN1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=SSO0857;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK41148.1; -; Genomic_DNA.
DR   PIR; E90236; E90236.
DR   RefSeq; WP_010923143.1; NC_002754.1.
DR   AlphaFoldDB; Q97ZN1; -.
DR   SMR; Q97ZN1; -.
DR   STRING; 273057.SSO0857; -.
DR   PaxDb; 273057-SSO0857; -.
DR   EnsemblBacteria; AAK41148; AAK41148; SSO0857.
DR   GeneID; 8761288; -.
DR   KEGG; sso:SSO0857; -.
DR   PATRIC; fig|273057.12.peg.869; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   InParanoid; Q97ZN1; -.
DR   PhylomeDB; Q97ZN1; -.
DR   Proteomes; UP000001974; 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   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; 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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..625
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151656"
FT   MOTIF           117..127
FT                   /note="'HIGH' region"
SQ   SEQUENCE   625 AA;  71387 MW;  38893F7E4602C19F CRC64;
     MDIIGRAKKE LAEYVAAQLG ISEEEVFKNI TYPPREELGD LSLALPSLIK GNINEKAKLL
     QEYKGELIER IEVAGIYLNA RLNLRNIFVS IFSKLDDSYG LEKIEKPKRI VVEHTSANPI
     HPLHIGHLRN TILGDALARA LKARGHSVNV RFYVNDTGRQ VAVLIYGLKL LGFPDPEPNV
     KKDLWLGIIY AMTNVILEIR KLREELKKLS ESEYREKVRE LDELIVIAND LRNRNEVLFD
     KLADAINAKE EPEKEIGEII KKYEEGNDEL KGIIRKYISY ALEGFSETLS KLNIRFDNFD
     YESDLLWENM VNEVLKALLS SSAKIPYKGV IALDLDSFLG DEARSKLRIP KGLKIPPLVL
     MRSDGTTLYT VRDIAYTIFK FNQFNADFVI NVIAEEQYIP QIQLRGALEL LGYSRFAENL
     LHYSYGMVNI QGLRMSGRLG KIITIDEIYE KLDNIVRNKL KEKGGNMENI DDIANAALRY
     AILSVSANKP LSFDLNRITS FEQNSGPYLQ YTYARAANIL AKSTENLSMD KVDFSDLVGD
     KRNILILIAK FPEVFKNAVD NLRLEDLVAF LRELSDIFNS WYDKERVLQE QDPRKRMLRL
     YIVKGVSVVL KNGLSVLGIR SLERM
//