ID A0A172Q9J8_9STRE Unreviewed; 563 AA.
AC A0A172Q9J8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ORFNames=A0O21_09335 {ECO:0000313|EMBL:AND80183.1};
OS Streptococcus pantholopis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1811193 {ECO:0000313|EMBL:AND80183.1, ECO:0000313|Proteomes:UP000077317};
RN [1] {ECO:0000313|EMBL:AND80183.1, ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|EMBL:AND80183.1,
RC ECO:0000313|Proteomes:UP000077317};
RX PubMed=27226124; DOI=10.1099/ijsem.0.001189;
RA Bai X., Xiong Y., Lu S., Jin D., Lai X., Yang J., Niu L., Hu S., Meng X.,
RA Pu J., Ye C., Xu J.;
RT "Streptococcuspantholopis sp. nov., isolated from faeces of the Tibetan
RT antelope (Pantholops hodgsonii).";
RL Int. J. Syst. Evol. Microbiol. 66:3281-3286(2016).
RN [2] {ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|Proteomes:UP000077317};
RA Bai X.;
RT "Streptococcus antelopensis sp. nov., isolated from the feces of the
RT Tibetan antelope (Pantholops hodgsonii) in Hoh Xil National Nature Reserve,
RT Qinghai, China.";
RL Submitted (MAR-2016) 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,
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; CP014699; AND80183.1; -; Genomic_DNA.
DR RefSeq; WP_067064548.1; NZ_CP014699.1.
DR AlphaFoldDB; A0A172Q9J8; -.
DR STRING; 1811193.A0O21_09335; -.
DR KEGG; spat:A0O21_09335; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000077317; 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; cd07956; Anticodon_Ia_Arg; 1.
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; 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|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Cytoplasm {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:UP000077317}.
FT DOMAIN 1..83
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 450..563
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 121..131
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 563 AA; 63271 MW; 336E95055DC64747 CRC64;
MDTKYLIAEK IKEAVPDLEL SAITNLLEVP KNSDMGDWAF PAFTLAKSWR KAPQMIASEI
AEKIDSEDFE KVEAVGPYIN FFLNKNKLSA DLIAQVISQG SDYGRQDLGE GGSVTIDMSS
PNIAKPFSIG HLRSTVIGDS LSMIFQKLGY QTIKINHLGD WGKQFGLLIL AYKKWGQEEA
VKAHPIKELL ELYVRINAEV QNHPELDDQA REWFRKLEAG DEEALELWQW FREESLLEFS
HLYDQLGVTF DSYNGEAFYN DKMAEIIDLL TANGLLQESQ GAQVVNLEKY GMEHPALIKK
SDGATLYITR DLATALYRKR QYQFAKSIYV VGNEQAAHFK QLKAILKEMG YDWSDDIVYV
PFGLVTKGGK KLSTRKGNII LLEPTLAEAI KRAADQINAK NPDLANKDAV AHAVGVGAIK
FYDLKSDRMN GYDFDLEAMV SFEGETGPYV QYAHARIQSI LRKAAFSPDA AATYSLNDKE
SWDIIKLIQA FPDVINRAAD RFEPSLIAKH AIHLAQSFNK YYAHTRIIAE DAERDSRLAL
CYATATVLKE ALRLLGVEAP NEM
//
