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Database: UniProt
Entry: SYR_SULAC
LinkDB: SYR_SULAC
Original site: SYR_SULAC 
ID   SYR_SULAC               Reviewed;         618 AA.
AC   Q4J904;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=Saci_1396;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80726.1; -; Genomic_DNA.
DR   RefSeq; WP_011278228.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4J904; -.
DR   SMR; Q4J904; -.
DR   STRING; 330779.Saci_1396; -.
DR   GeneID; 78441741; -.
DR   KEGG; sai:Saci_1396; -.
DR   PATRIC; fig|330779.12.peg.1345; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   Proteomes; UP000001018; 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; 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; 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; 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..618
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151655"
FT   MOTIF           113..123
FT                   /note="'HIGH' region"
SQ   SEQUENCE   618 AA;  71087 MW;  11C9ACB100739ABA CRC64;
     MNPIRSVKEE FCEIVANGLG ISKDVIFKTL EYPPREELGD ISLPLPSLKL NVRTEVTFSH
     GKLIKEVRKT GIYVNAFVDE KELFKLLFTE MQDDYGVEKT ENPKRIVVEH TSANPIHPLH
     IGHLRNSILG DTISRMLKIR GHDVNRRFYV NDAGRQVAIL TLGYILLGEP EPSPKVDHWF
     GLIYSITNVI IEIRELKEEL KKDLDPDTYK DKINRLDELV ATAQSLRERN PEFFDKLADA
     INSIPDVESE IQKIIKSYEK GDDPKIKQIV RKIVNLNLDG FRESLDKLEI SFDVYDYESE
     LLWSGMVDEI LSKAFQIAKD YKGTKALELE DINEKIKEIL NIPKGLKLPP LVLTRSDGTS
     LYTTRDIAYT VKKFSDFKAD TVINVIAEQQ SIPQMQLRAS LYLLGYERLA QNLVHYSYGM
     VNLQGMRMSG RLGRFISLDD VIEKVSEVAK KKIEEKSGDI TNLRDIVNSA IRYAILSVAS
     NKPVTFNINN IVDFEQNSGP YLQYTYARAY NILAKNQDEI KLTDADLSDL IGDKRRLLLL
     IARFPETFNK AIDELRPEDL IDFLRRTADV FNRWYNFERV LQEPDYRKRI TRLFIVKGIE
     RVLYNGLNAL GIKPLSKM
//
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