SYR_PYRAR
ID SYR_PYRAR Reviewed; 630 AA.
AC A4WLP0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=Pars_1756;
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-2007) 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; CP000660; ABP51307.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WLP0; -.
DR SMR; A4WLP0; -.
DR STRING; 340102.Pars_1756; -.
DR EnsemblBacteria; ABP51307; ABP51307; Pars_1756.
DR KEGG; pas:Pars_1756; -.
DR HOGENOM; CLU_006406_6_1_2; -.
DR OMA; NKPLHLG; -.
DR PhylomeDB; A4WLP0; -.
DR Proteomes; UP000001567; 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; -; 1.
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.
FT CHAIN 1..630
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018097"
FT MOTIF 120..130
FT /note="'HIGH' region"
SQ SEQUENCE 630 AA; 71544 MW; DC8A880FD4D58C43 CRC64;
MDPLKLPKQE FADALGKISS RLGLAEVPEI EKTRRYGYFS ARFHKYKIDP TRLRDAVEEL
SNAGFQYISG LSAEGLYVNA DLNAKRLGEL VFEAVAKMGK KYGFTEECQL GSFLVEHTSA
NPIHPLHIGH GRNAILGDSL ARLLRFCDNR VEVHFYVDDC GVQVMYATIG YNAVRDEARE
WIERAKPDLV VGHIYSATNA VAEIGRLKKE AERAQDDEHK RSLIGEIDEW VAVLKRLMES
EGDLVAKVVE RLGQRDVAGE AVELNRRYEA GDPEAKRVVR EVVDLVLRGQ RETLARLGIE
IDRWDYESEL AVWSGEASRI VEELQRRWPQ YVEYKGGAVV FRADKFVDDF KLWDVLDLPK
FIPPVTLTRS DGTTLYVTRD VAYALWQARQ GFDKVVRVIS TEQTHEQAHV RIILYALGFE
DVAKKIVHYA YEMVNLPGMK MSARRGRYIS LDEILDEAAE RSASLVKEKS PEIAGVIAEK
VGVGSVRYAF LSTSPRKPIE FRWEVVLNLR QNSGTFLQYT YVRAYSILEK APDVERASVP
EQMLEEEKEL LVKIAEWPSV VREAVRALRP DYVAEYLDGL ALLFNSYYEK APVLKAVEGV
RKFRIALVNA VKTVLEAGFY ILGIPTLTKM