ID A0A1X7FND1_9ACTN Unreviewed; 352 AA.
AC A0A1X7FND1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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=SAMN02745830_04351 {ECO:0000313|EMBL:SMF54694.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF54694.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF54694.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF54694.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWZW01000009; SMF54694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7FND1; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000192930; 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:SMF54694.1}; 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:UP000192930}.
FT DOMAIN 4..92
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 226..352
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 150..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 37550 MW; 628D53D694AC2C20 CRC64;
MTPVELSRTV LGAVRRAVDA GELRVDVPER VVVAPPGPGG VGDFATNIAL QLARPAGQPP
LRVAELLRPH LVGVDGITGV EITGPGFLNI RLDQGVGTAL VRRILDEGAA RYGHSDTLAS
QVYVLRVPYE VRAEVVADVL ARMVSSQGAR VEIQHQKHQK HQKQQKHPKG DKHETVDVRP
VPVPEDPAPL GPDAARWALL HPAPSDRPRI TADHLVQREG NPLFRVRYAH ARTRAVVRNA
ADLGFTPEPG TPEPGTPLLP LLTDYPRILA TAAPLPRLSR LPRPDGIAAP SRLARHLVAV
ADAVLDLLPA TLPRGDEKPS AAHRARLALA EAAGTVLAGG LSLLGIDAPD HL
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