ID   SYR_PYRAB               Reviewed;         625 AA.
AC   Q9V0V2; G8ZJF0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=PYRAB06880; ORFNames=PAB0469;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ248285; CAB49601.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70077.1; -; Genomic_DNA.
DR   PIR; H75110; H75110.
DR   RefSeq; WP_010867806.1; NC_000868.1.
DR   AlphaFoldDB; Q9V0V2; -.
DR   SMR; Q9V0V2; -.
DR   STRING; 272844.PAB0469; -.
DR   GeneID; 1495590; -.
DR   KEGG; pab:PAB0469; -.
DR   PATRIC; fig|272844.11.peg.722; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   OrthoDB; 372102at2157; -.
DR   PhylomeDB; Q9V0V2; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; cd07956; Anticodon_Ia_Arg; 1.
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; IPR001412; aa-tRNA-synth_I_CS.
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:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..625
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151650"
FT   MOTIF           128..138
FT                   /note="'HIGH' region"
SQ   SEQUENCE   625 AA;  71691 MW;  F1B1E7D79AFEC891 CRC64;
     MLSRVKEGAR EKIIKVIESL APGWKGEIEF KDTPSPELGD FGTPVAFKLA RVMKKPPFQI
     AELIVEELKK ELPEGIREVR AINGYVNFFV DYGYLARQLI VEVLEKGDRF GSSDIGRGKK
     VIVEHTSVNP TKPLHMGHAR NAILGDSMAR ILRFLGYEVE VQNYIDDLGI QFAQVYWGYL
     KLREKFEKIM KELKEKGIKE DPIDHVLGLL YVEVNRVLEE NPEIEAEIRD IMKKLESGEL
     NGRELAESVV RAQMVTTYRL GIKYDLLVWE SDIVSRKLFE IAVKLLERNE NFYTPNEGKY
     KGAFVMDLSK LFPDMKNPYL VLRRSDGTAT YTGKDIAYHL WKFGKIDVDL LYKPWDEHTW
     TTAPDGESVK GKFGGADIVI NVIGAEQRHP QMAIKHALKL LGFEDAAENL HHLAYEHVER
     PEGKFSGRKG TWVGFTVDEV INEAIKRARE LIEEKSPGLS DEEKEEIAEK VGVGAIRYNM
     VKYSPDKKII FRWEDVLNFE GESAPYIQYA HARCSSILRK AGNPEWEALL KEANFKELTE
     RERELIILLS KFPEVVEQAG RDVKPHLIAW YANELASLFN KFYMDHPVIK AEKGIREARL
     LLVMAVRQVL RNSLWLLGIE APDRM
//