ID L7VG46_9FLAO Unreviewed; 581 AA.
AC L7VG46;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN Name=argS {ECO:0000313|EMBL:AGC66940.1};
GN ORFNames=ASNER_180 {ECO:0000313|EMBL:AGC66940.1};
OS Candidatus Uzinura diaspidicola str. ASNER.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Candidatus Uzinura.
OX NCBI_TaxID=1133592 {ECO:0000313|EMBL:AGC66940.1, ECO:0000313|Proteomes:UP000011174};
RN [1] {ECO:0000313|EMBL:AGC66940.1, ECO:0000313|Proteomes:UP000011174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASNER {ECO:0000313|EMBL:AGC66940.1,
RC ECO:0000313|Proteomes:UP000011174};
RX PubMed=23279075; DOI=10.1111/1462-2920.12058;
RA Sabree Z.L., Huang C.Y., Okusu A., Moran N.A., Normark B.B.;
RT "The nutrient supplying capabilities of Uzinura, an endosymbiont of
RT armoured scale insects.";
RL Environ. Microbiol. 15:1988-1999(2013).
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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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DR EMBL; CP003263; AGC66940.1; -; Genomic_DNA.
DR AlphaFoldDB; L7VG46; -.
DR STRING; 1133592.ASNER_180; -.
DR KEGG; udi:ASNER_180; -.
DR PATRIC; fig|1133592.3.peg.168; -.
DR HOGENOM; CLU_006406_6_1_10; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000011174; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00456; argS; 1.
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 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; 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.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000011174}.
FT DOMAIN 6..88
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 460..581
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 581 AA; 68254 MW; 91FCFD5030950C08 CRC64;
MKTTLAIFRL IVMRAIASIY IEGITSNIEL KTTKKEFRGH ITLVLFPLVK IIKKPLKQIG
KEIGEYVKKH LIIVHSFHLL NGFLNFECSE EYYFKLLKKI SKEILFLKSS EEDSLMIEYS
SPNTNKPLHL GHIRNHLLGN SISEIFKAFG HNVIKIQIIN DRGIHICKSM LAWKKFSSGE
TPEITFKGDH LIGKYYVAFE KAYKKEVEDL CAKGYEKELA EKQAPIMQEV RKLLLLWEKR
NVKTWYHWRN MNSWAYEGIE QTYCSLGIYF DDTQYESKTY LLGKSIIEDG LKKGVFYKKE
DGSVWVDFTN VGLDEKLLLR SDGTSVYITQ DLGTAVERFE LYSIKSLIYI VGEEQEYHFK
VLFLILKYMR YAWADRLFHL SYGLVQLLSG KMKSREGIII DADNLIDEMH KLAQFLTYQK
ENTLGIGALK YFLLKIDTKK RILYHTKSSI DFNGNTGPYI QYTNARISSL YRKAFTKMYW
RNSMIRYYRY SIIGRYEKYL LKYMEQYTEA LLLAKKCLIP SIIANYAYNL SKTFNDFYQN
VCIINIKNKY DFVFRLFLSK KCGNCLKKTM NLLGIEMPEY V
//
