SYR_DEHM1
ID SYR_DEHM1 Reviewed; 556 AA.
AC Q3Z717;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=DET1270;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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 -!- SUBUNIT: Monomer. {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; CP000027; AAW39452.1; -; Genomic_DNA.
DR RefSeq; WP_010936959.1; NC_002936.3.
DR AlphaFoldDB; Q3Z717; -.
DR SMR; Q3Z717; -.
DR STRING; 243164.DET1270; -.
DR PRIDE; Q3Z717; -.
DR EnsemblBacteria; AAW39452; AAW39452; DET1270.
DR KEGG; det:DET1270; -.
DR PATRIC; fig|243164.10.peg.1199; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_0; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000008289; 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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..556
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242012"
FT MOTIF 133..143
FT /note="'HIGH' region"
SQ SEQUENCE 556 AA; 61770 MW; 543E53BA2F72AE14 CRC64;
MNSILAIKNI IIESLSQALE KARQEGQIPA LSVDISIEHP QKTNYGDYAT SLPLRLAKAT
GKRPMELAEI LAGYIEPGEG IAKVSVAPPG FINFTFSKEW LCNLVKTILG EAESYGNINM
GGGSRVQIEF VSANPTGPIH IGHGRGAVLG STLSNVLKAA GYYVEEEFYI NDAGSQIDAF
KRTLFARYQQ ALGKEAAVPQ DGYHGQYMVE LAAEMVAKYG DKYLQMPLEI AQNDLGEIGM
ARMLCLISDD LKSLKVDFDV WFSERSLYSG GQYKTAMDIL LANNYIAERD NATWFSSTLL
GDSKDNVIVR SDGTPTYFAS DIAYHYNKFI ERKFDRVINI WGADHQGHVS RMKAMLSALG
INPERLTTLL FQMITLKRGG ELVRLSKRTG EMISLSEVIE EVGADACRFF FLSRSTESQM
DFDLELAKKE SAENPVYYVQ YAHARICSIL SLAKEKGLSY SGGDTALLGE EAELELIRKM
AELPEIVETV ARTLEPHHLT YYAQELANAF HQFYKDCRVI SDNTELSSAR LKLVDASRIV
LARTLHLMGM TSPQSM