SYR_METAR
ID SYR_METAR Reviewed; 563 AA.
AC Q0W6L7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=UNCMA_22090;
GN ORFNames=RCIX568;
OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=351160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX PubMed=16857943; DOI=10.1126/science.1127062;
RA Erkel C., Kube M., Reinhardt R., Liesack W.;
RT "Genome of rice cluster I archaea -- the key methane producers in the rice
RT rhizosphere.";
RL Science 313:370-372(2006).
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; AM114193; CAJ35976.1; -; Genomic_DNA.
DR RefSeq; WP_012036529.1; NC_009464.1.
DR AlphaFoldDB; Q0W6L7; -.
DR SMR; Q0W6L7; -.
DR STRING; 351160.RCIX568; -.
DR EnsemblBacteria; CAJ35976; CAJ35976; RCIX568.
DR GeneID; 5144438; -.
DR KEGG; rci:RCIX568; -.
DR PATRIC; fig|351160.9.peg.2259; -.
DR eggNOG; arCOG00487; Archaea.
DR OMA; NKPLHLG; -.
DR OrthoDB; 7046at2157; -.
DR Proteomes; UP000000663; 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; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
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..563
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018142"
FT MOTIF 119..129
FT /note="'HIGH' region"
SQ SEQUENCE 563 AA; 63244 MW; B6BE5762112717D7 CRC64;
MYLKLLEEAG RLMKQAVADA GYTVEDMSLV ESQHADVSSS LPFRLAKELK KNPKEIAAAI
VEKMGKSEYI DRVEATGAYI NFYASQKYIT DSLKEILSEK KFFELEPNGI KVILEHTSAN
PTGPLHVGRG RNPIIGDTLA RLLRAGGYDL EVQYYVDDMG KQEATIVWGY DHLDRIKPGK
PDTDKPDHEI VEVYRAATDL RKSDEAVEKE ISEILNAYEH MDPATAVKFR EMVERCLEGQ
KMTLARMNVF YDRFVWESDF VRDGSVNKAV KKLAESQYAT TKDGALALDL SSFGMDKEFV
LTRADGTSLY TTRDIAFHVW KLARCDRAIN VLGEDQKLAM QRLNAALSIL GEKKAPTIVF
YSFVSLPEGR MSTRKGVVVN LDDLLDEAVE RAYVEVDKRR KDIPEEKKRQ IAEAVGIGAV
RFDIVRVAPE KSITFKWETA LDFEKQGAPF IQYAHARCCS ILEKAKPGEY DASMLREPEE
AALVKKIAMM PYVIKNASTE LKPHVIAIYA RELAEAFNQF YRVSPVLIAE PELKEARLAL
VEASRKALAA SLGMLGIAAI EEM