ID A0A090AQT7_9ENTR Unreviewed; 574 AA.
AC A0A090AQT7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123,
GN ECO:0000313|EMBL:BAP58712.1};
GN ORFNames=TGUWTKB_4860 {ECO:0000313|EMBL:BAP58712.1};
OS Candidatus Tachikawaea gelatinosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Tachikawaea.
OX NCBI_TaxID=1410383 {ECO:0000313|EMBL:BAP58712.1, ECO:0000313|Proteomes:UP000031627};
RN [1] {ECO:0000313|Proteomes:UP000031627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UwTKB {ECO:0000313|Proteomes:UP000031627};
RA Kaiwa N., Hosokawa T., Nikoh N., Meng X.Y., Tanahashi M., Moriyama M.,
RA Maeda T., Yamaguchi K., Shigenobu S., Ito M., Fukatsu T.;
RT "Symbiont-containing voluminous jelly as an extraordinary maternal gift for
RT overwintering insect nymphs.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAP58712.1, ECO:0000313|Proteomes:UP000031627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UwTKB {ECO:0000313|EMBL:BAP58712.1,
RC ECO:0000313|Proteomes:UP000031627};
RA Kaiwa N., Hosokawa T., Nikoh N., Tanahashi M., Moriyama M., Meng X.Y.,
RA Maeda T., Yamaguchi K., Shigenobu S., Ito M., Fukatsu T.;
RT "Symbiont-Supplemented Maternal Investment Underpinning Host's Ecological
RT Adaptation.";
RL Curr. Biol. 20:2465-2470(2014).
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 ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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DR EMBL; AP014521; BAP58712.1; -; Genomic_DNA.
DR RefSeq; WP_041063255.1; NZ_AP014521.1.
DR AlphaFoldDB; A0A090AQT7; -.
DR STRING; 1410383.TGUWTKB_4860; -.
DR KEGG; sbw:TGUWTKB_4860; -.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000031627; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 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|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Reference proteome {ECO:0000313|Proteomes:UP000031627}.
FT DOMAIN 5..87
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 458..574
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 123..133
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 574 AA; 66292 MW; 86D04D1013A11825 CRC64;
MNTHAFISNK VREAMTSINI PEDFDPQVKQ TNRIKFGHYQ VNGIISIAKK LKKSSFSLAN
ELILKIDLQG IAKNITVIKP GFINIYLDEN WLSIQLEKIF CSSRLSINVV KKPQTIVIDY
SSPNLAKEMH VGHLRSTIIG DSSARILEFL GHKVIRMNHV GDWGNQFGML IAYIIKKKIQ
DISLINLEKI YKKSKILYEQ DINFNSESRN CLKQLQSGNV LHKKIWKKIV KVSLNNNQKI
YNRLNVSLKD QHVLGESFYH NDLSKIVKDL KEKKLAEESE GAIVVFLKEY INKNGQPFGV
IIQKKDGGFL YTTIDIACLK YRYETLKADR ILYYIDARQH LHLMQVFNIA LKANYITADL
QLEHHAFGMI LNDNKQPFKT RSGNTIKLID LLNEGYKKAF KLIQMKNPCM KDLEKQKLAE
IISISAIKYA DLSRNRTHDY IFNWDLMLSF EGNTAPYIQY AYTRILSILK KSFVKNHEIN
NKIIISNTYE MQLAICLLQF EETIEKTAFL GTPHLICTYL YKISGLFSIF YENCPIINNK
KMNIKKSRLK LAIITAKIIK LGLDLLGIQT IKHM
//
