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Database: UniProt
Entry: A0A0G1QX05_9BACT
LinkDB: A0A0G1QX05_9BACT
Original site: A0A0G1QX05_9BACT 
ID   A0A0G1QX05_9BACT        Unreviewed;       556 AA.
AC   A0A0G1QX05;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   ORFNames=UX20_C0029G0005 {ECO:0000313|EMBL:KKU13180.1};
OS   Candidatus Magasanikbacteria bacterium GW2011_GWC2_45_8.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1619050 {ECO:0000313|EMBL:KKU13180.1, ECO:0000313|Proteomes:UP000034911};
RN   [1] {ECO:0000313|EMBL:KKU13180.1, ECO:0000313|Proteomes:UP000034911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
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:KKU13180.1}.
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DR   EMBL; LCLH01000029; KKU13180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1QX05; -.
DR   STRING; 1619050.UX20_C0029G0005; -.
DR   Proteomes; UP000034911; 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   Gene3D; 3.40.50.620; HUPs; 1.
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.
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   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}.
FT   DOMAIN          7..90
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          440..556
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   556 AA;  61596 MW;  30839DA927E0F7F1 CRC64;
     MKKHPLHIIK SAIVEDLKKH HAFLGALAED ALVYPPDTKF GDIALPCFAY AQSAGKNPAE
     LARAIAESGV VASEWVSAVN AAGPYVNFVL KGDALARVLF AALKKPALFG TNDFGKGERV
     MIEYPSPNTH KEFHIGHVRN VCLGVALTHL YEASGFKMAQ VDYTNDLGSH VAKCLWALMK
     FHKGEKPPRG REARWLGAVY AEGAQKLEAH PEYAPEVSEV LQKLESRDKV VHTLWKKTRA
     WSIKGMNDEV KDEGKKIVAE LLKKGIAKKS QGAVIIDMEA QGFGIMLLLK SDGTGLYSTS
     DLALARKKFK LFKIDRSINI TDVRQSLYFK QLFHALALSG FTQKMTHIGY EFVRLPEGAM
     ASRTGRVILY EDMRDEIIEA AAEETKKRHP EWSARKIADT AHALALAGLK FGMLKYDPNK
     VIVFDKKEAL SFEGFTGPYL LYTFARMNSL LKKTRSVARG LVDAALLADA HEKQLAIHAA
     RLPEIVQSAT ENNNPSELAQ YAYKLCQLFG GFYEHCPVLR APNEDVGRAR IALVQAAQSV
     LEQSLKLLGI PLIQEM
//
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