SYR_PYRIL
ID SYR_PYRIL Reviewed; 632 AA.
AC A1RS32;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Pisl_0586;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) 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: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; CP000504; ABL87764.1; -; Genomic_DNA.
DR RefSeq; WP_011762340.1; NC_008701.1.
DR AlphaFoldDB; A1RS32; -.
DR SMR; A1RS32; -.
DR STRING; 384616.Pisl_0586; -.
DR PRIDE; A1RS32; -.
DR EnsemblBacteria; ABL87764; ABL87764; Pisl_0586.
DR GeneID; 4616557; -.
DR KEGG; pis:Pisl_0586; -.
DR eggNOG; arCOG00487; Archaea.
DR HOGENOM; CLU_006406_6_1_2; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 7046at2157; -.
DR Proteomes; UP000002595; 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; 3.40.50.620; -; 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 PANTHER; PTHR11956; PTHR11956; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..632
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018098"
FT MOTIF 120..130
FT /note="'HIGH' region"
SQ SEQUENCE 632 AA; 72117 MW; 3A481240A6BC3E5F CRC64;
MDPLKPPREE FEKFVAEVAY AIGIGEVPEI ERSKRFGYFS AKFHKYRVDA GKLKETVDSL
KSRQFKYLTS ISVDGLYLNV DLAVEKVAEL TFRAVAEMGD KYGFTDECKI GSFLVEHTSA
NPIHPLHIGH GRNAILGDSL VRLLRFCGNV VQSHFYVDDC GVQVMYAAIG YNVVKKYVDE
VLKRTKPDVV IGAIYSAVNA IAEINRLKKE LEKEKDDEKR REIINEIDSW VSVLKRLIDT
EGEVINKLVE VLGQRNIVEE AAELNKRYET GDPEVKKIVR EVVELVLKGQ RETLARLGIE
LDSWDYESDI AVWSGEATRV VSELRRRWPQ YIDDRGGAVV FRADKFVEDF KLWDVLDLPK
FIPPVTLTRS DGTTLYVTRD VAYALWQARR GFDKVIRVIS TEQTHEQAHV RIILYALGYE
DVAKKLIHYA YEMVNLPGMK MSARRGQYIS LDEILDEAVE RSADLVKEKN PEIAGIIAER
VGVGSVRYAF LSTSPRKPIE FKWETVLNMR QNSGPFLQYT YVRAYSILEK AQEIDLKKVA
IPKEILPEER ELILKVAEWP SVVREATRAL RPDYVAEFLD GLALIFNSYY EKAPVLKTEE
PVRSFRLALV NSVKTVLAAG FYILGIPTLT KM