SYR_PYRAE
ID SYR_PYRAE Reviewed; 630 AA.
AC Q8ZTA8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=PAE3343;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64855.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZTA8; -.
DR SMR; Q8ZTA8; -.
DR STRING; 178306.PAE3343; -.
DR EnsemblBacteria; AAL64855; AAL64855; PAE3343.
DR KEGG; pai:PAE3343; -.
DR PATRIC; fig|178306.9.peg.2519; -.
DR eggNOG; arCOG00487; Archaea.
DR HOGENOM; CLU_006406_6_1_2; -.
DR InParanoid; Q8ZTA8; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002439; 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 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; 2.
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; Reference proteome.
FT CHAIN 1..630
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151651"
FT MOTIF 120..130
FT /note="'HIGH' region"
SQ SEQUENCE 630 AA; 71667 MW; 40A1D80199267641 CRC64;
MDPLRQPREE FVKVLGEVSR ELGLPEVPEV ERTRRYGFFS ARFHKYKVDH SRLAEVVNLI
KNKRFEFLSS LSVDGLYLNA DLNVSKVAEL VFEAVVKMGR KYGFTEECVT GSYLVEHTSA
NPVHPLHIGH GRNAILGDSL ARLLKFCGNK VETHFYVDDC GVQVMYAAMG YNAVKDEVKK
RIEKSKPDVV IGHVYSATNA VAEIGRLKKE LEKAQDDERK REILREIDEW VAVLKRLMDS
EGDIISKIAE ELGRRDLLNE AVELNRRYES GDPEAKGVVR EVVDLVLKGQ RETLARLGVE
IDKWDYESEL TVWSSEAMRI VSELQKRWPQ YIEIKGGAVV FRADKFVQDY NLWDVLDLPR
FIPPVTLTRS DGTTLYVTRD VAYALWQARQ GFDKVIRVIS TEQTHEQAHV RIILYALGYV
DEAKKIVHYA YEMVNLPGMK MSARRGQYIS LDEILDEAAE RSASLVKEKN PEVSGVIAER
VGVGSVRYAF LTTSPRKPIE FKWDVVLNLR QNSGTFLQYT YVRAYSILEK AGEIGNVPVP
ENMLAEEREL VLKIAEWPSV VKEAAKSLRP DYVAEYLDGL ALVFNSYYEK APVLKAEESV
RGFRIAIVNA VKTVLEAGFY ILGIPTLTKM