SYR_AERPE
ID SYR_AERPE Reviewed; 644 AA.
AC Q9YB39;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 128.
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=APE_1756;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA80759.1; -; Genomic_DNA.
DR PIR; B72559; B72559.
DR AlphaFoldDB; Q9YB39; -.
DR SMR; Q9YB39; -.
DR STRING; 272557.APE_1756; -.
DR EnsemblBacteria; BAA80759; BAA80759; APE_1756.
DR KEGG; ape:APE_1756; -.
DR PATRIC; fig|272557.25.peg.1181; -.
DR eggNOG; arCOG00487; Archaea.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002518; 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; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
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; PTHR11956; 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; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 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..644
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151642"
FT MOTIF 129..139
FT /note="'HIGH' region"
SQ SEQUENCE 644 AA; 72173 MW; 076E18F55C0B5A08 CRC64;
MASSIDPLTR LHGILSSYLS EVLGVDRSVV ERLLAPPPRK EYGDLGFPLM RFARSSNASA
DSIVESLRGK LWERGITWAS PTLEAGYLNI VFDVEKLGDE VFRLLASGWR PSTARTSRPE
TIVVEHTSAN PIHPLHLGHA RNSSLGDALA RLLEARGHRV NRRFYVDDVG RQAVVASLGF
KLSGVTPREL ASRMGVKVDH AVGWVYAVTH NALETVTARK RGDTSKVDEA LSTLARLKER
GDREVFDRIL EAVGSLDDPE GLVSEMMRKY ERGEEPEKSL IRGVVSAVLE GFRETLGRFG
VDFDDWDWES DLLWSGLVNK IIEEARRSPF LTTHKDAIAL DIPRIVREVL ARDPEAASTI
KLPRSLEIPP LILVRSDGTT LYTTRDLAYS VYKFRVTGAD RVINVIGADQ RLPQLQIRLA
LLGLGYRREA LNMMHYDYEI VSLPGRRMSS RRGEYVTLDE LLEMAKARSV REVESRNPGA
DRDWIESTAE KIAVGAVRFA LVRPGRLKPI TLDVERILDL KENTAPYLQY TYARASSILE
KHGEIDYLKA HPASLEEGSR RELFVEALRF PLVSAKAADD LAPEDLASYL LRLADMFNSW
YQKDSVIHEE WEGARHAKAA LVLLVKSVIG EGLRLLGVEP LEKM