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Database: UniProt
Entry: A0A0M9YE82_9ACTN
LinkDB: A0A0M9YE82_9ACTN
Original site: A0A0M9YE82_9ACTN 
ID   A0A0M9YE82_9ACTN        Unreviewed;       345 AA.
AC   A0A0M9YE82;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   ORFNames=ADK54_19710 {ECO:0000313|EMBL:KOU42381.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU42381.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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:0000256|ARBA:ARBA00001766};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOU42381.1}.
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DR   EMBL; LGDD01000246; KOU42381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9YE82; -.
DR   PATRIC; fig|1415557.3.peg.4373; -.
DR   Proteomes; UP000037774; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          25..112
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          231..345
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   345 AA;  36736 MW;  39B68412AB6F7F98 CRC64;
     MAKPVRGGTP LLPYAGPVTP AELSRTVVRV VRSAVDEGAL SVAGDVVPDA VKVERPRPGG
     GGDYASGVAL KLAAAAGLPP RRVAEVLRRR IADQPGIALV EISGPGFLNI TLDRGGKDRV
     VRRVLEATAS YGHGDALLGQ SYDFAEAREE RARVVTDVVV RLLRSQGALA RTVEHGGQVL
     PLVACPEPRL RELVGVDAAR WAMLRPARHD RPRIEVDELL AQRESNALFR VRYAYARSRA
     LTRNALELGF RGEVGPVPDG EILLGLLSDH PGVLESAARH QAPDRLARQL EAVADGLLRF
     QHGVLPLGDE KPSAAHRNRL ALAEAAGTVL AGGLSLLGID APEFL
//
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