ID A0A1Z1WIZ9_9ACTN Unreviewed; 337 AA.
AC A0A1Z1WIZ9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=SMD44_05897 {ECO:0000313|EMBL:ARX86425.1};
OS Streptomyces alboflavus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX86425.1, ECO:0000313|Proteomes:UP000195880};
RN [1] {ECO:0000313|EMBL:ARX86425.1, ECO:0000313|Proteomes:UP000195880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK44 {ECO:0000313|EMBL:ARX86425.1,
RC ECO:0000313|Proteomes:UP000195880};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT "Streptomyces alboflavus Genome sequencing and assembly.";
RL Submitted (MAY-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; CP021748; ARX86425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z1WIZ9; -.
DR STRING; 67267.GCA_000716675_04656; -.
DR KEGG; salf:SMD44_05897; -.
DR eggNOG; COG0018; Bacteria.
DR Proteomes; UP000195880; Chromosome.
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:ARX86425.1}; 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:UP000195880}.
FT DOMAIN 4..79
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 222..337
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 35527 MW; 3B1FAF6DFF0032CD CRC64;
MRRAVDAGEL SATVPDDAHV ERPRPGGTGD YATNLALRIA KEAGAPPRRV AELLSARLTA
EPGIAHAEAT GPGFVSITLD PHGTPALVAE IREQGESYGH VARDTGALVQ LHTPHDLRAL
VVADAARRIL RSQGALVRVT SDEAPDERWV EVAGVRVDAY GRPPTPLTTL RPVPPTPGGP
DPLDLGPDAA RWALLHPAPH DRPHTDPGQH LAQHESNPLF RIRYAYARTR ALTRNAADLG
FTAAPGATDA SAHDLLGALG DHPTVLATAA RRHAPDRLTR HLVRTADAFL AQAHTVLPLG
DEKPSAAHRS RLALAEAAGT VLAGGLSLLG ISAPEYL
//
