ID A0A2U9IIX4_9CREN Unreviewed; 620 AA.
AC A0A2U9IIX4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN ORFNames=DFR85_10710 {ECO:0000313|EMBL:AWR95992.1};
OS Acidianus brierleyi.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=41673 {ECO:0000313|EMBL:AWR95992.1, ECO:0000313|Proteomes:UP000248044};
RN [1] {ECO:0000313|EMBL:AWR95992.1, ECO:0000313|Proteomes:UP000248044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1651 {ECO:0000313|EMBL:AWR95992.1,
RC ECO:0000313|Proteomes:UP000248044};
RA Counts J.A., Kelly R.M.;
RT "Complete Genome Sequences of Extremely Thermoacidophilic, Metal-Mobilizing
RT Type-Strain Members of the Archaeal Family Sulfolobaceae: Acidianus
RT brierleyi DSM-1651T, Acidianus sulfidivorans DSM-18786T, Metallosphaera
RT hakonensis DSM-7519T, and Metallosphaera prunae DSM-10039T.";
RL Submitted (MAY-2018) 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:0000256|ARBA:ARBA00001766,
CC ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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DR EMBL; CP029289; AWR95992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9IIX4; -.
DR KEGG; abri:DFR85_10710; -.
DR OrthoDB; 372102at2157; -.
DR Proteomes; UP000248044; 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; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Reference proteome {ECO:0000313|Proteomes:UP000248044}.
FT DOMAIN 504..620
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 112..122
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 620 AA; 71190 MW; FED4FDF1F3EDAFAF CRC64;
MNIIREAKKE ASQIISKAIG INEDIILNNI EYPPKGDLGD LALPLPSVTK NFNVNVTGKG
YYIKNIERSG VFINIFLDES KIFTTIFSNF DEKYGIEKSE NPKKIVVEHT SANPIHPLHI
GHLRNSILGD TLVRLLRARG HDVNSRFYVN DSGRQVAILI YGLSKLNYPE PPSNIKKDEW
LGLIYAMTNV IIEIKKITDE LKNSGENEYK EKISKRDELV ATANELRERN QEYFDILTEN
IMKDIDPEKE ILEIIKKYET GDANTKVIVR KYVSYAIDGF LESLDRLHIS FDVFDYESDI
LWSGEVKQIL NIALDSPAKI NYKGTWALDL QNFIDDKTRE ELNIPKDLEL PPLVLMRSDG
TTLYTLRDVA YTFRKFSDFK ADIVINVIAE QQYMPQIQLR ASLYILGYPE YARNLLHYSY
GMVNLQGMRM SGRLGKYISL DDIYDKVKEV VETKIKEKKG NVENLNEIVN SAIRYAIVSV
SANKPISFNI SKITNLEENS GPYLQYTYAR AYNILSKVNE KLDLSKADLN ELSGDKRKIL
IMISKFPEIF GKAADDMKPE ILAIYLRQFS DLFNSWYDKE RVLQETDENK RTTRIYLVKG
VEGVLRNGLE ILGITPLSRM
//
