ID A0A1M7QU13_9ACTN Unreviewed; 337 AA.
AC A0A1M7QU13;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=SAMN05216499_14311 {ECO:0000313|EMBL:SHN35290.1};
OS Actinacidiphila paucisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310782 {ECO:0000313|EMBL:SHN35290.1, ECO:0000313|Proteomes:UP000184111};
RN [1] {ECO:0000313|EMBL:SHN35290.1, ECO:0000313|Proteomes:UP000184111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHN35290.1,
RC ECO:0000313|Proteomes:UP000184111};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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};
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DR EMBL; FRBI01000043; SHN35290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7QU13; -.
DR STRING; 310782.SAMN05216499_14311; -.
DR Proteomes; UP000184111; 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 ECO:0000313|EMBL:SHN35290.1}; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184111}.
FT DOMAIN 13..101
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 216..337
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 159..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 35884 MW; CE090A0BD663FE36 CRC64;
MLPLAYPFPV TPAELSWTVL STVRRAVAAD ELRVAVPEKI VVQRPPRPGC GDYATNVALQ
LAGQAGRSAY EVAGILAARL AREPGIAQVE VAGAGFLNIT LSARAYADVV RQVREQGADY
GRGEGLAGEG VTVVPEPPGA VRATMVADVV NGLLRAAGAG PGSRREGLTV AEGDGDPGRL
GRDAARWSLL RPPAEDPPRP GPALLAQREA NPLFRVRYAH SRTRALLRNA HDLGVRVEAA
ARDPYRHPAE TELLGLIADF PRVVETAARR RAPDRLARHL ERLADAYLRF QDECPVLPKG
DEKPSAVHAA RVRLADATGI VLADGLHLLG ISAPDHL
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