ID A0A347SU98_9LACO Unreviewed; 561 AA.
AC A0A347SU98;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=DS830_01730 {ECO:0000313|EMBL:AXX65607.1}, DS832_02275
GN {ECO:0000313|EMBL:RHW48439.1};
OS Bombilactobacillus bombi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1303590 {ECO:0000313|EMBL:AXX65607.1, ECO:0000313|Proteomes:UP000261753};
RN [1] {ECO:0000313|EMBL:AXX65607.1, ECO:0000313|Proteomes:UP000261753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI-2.5 {ECO:0000313|EMBL:AXX65607.1,
RC ECO:0000313|Proteomes:UP000261753};
RX PubMed=30249635; DOI=10.1073/pnas.1803880115;
RA Motta E.V., Raymann K., Moran N.A.;
RT "Glyphosate perturbs the gut microbiota of honey bees.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:10305-10310(2018).
RN [2] {ECO:0000313|EMBL:RHW48439.1, ECO:0000313|Proteomes:UP000284822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LV-8.1 {ECO:0000313|EMBL:RHW48439.1,
RC ECO:0000313|Proteomes:UP000284822};
RA Motta E.V.S., Moran N.A.;
RT "Genome sequences of six Lactobacillus spp. isolated from bumble bee
RT guts.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AXX65607.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BI-2.5 {ECO:0000313|EMBL:AXX65607.1};
RA Ferrada E.E., Latorre B.A.;
RL Submitted (AUG-2018) 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; CP031513; AXX65607.1; -; Genomic_DNA.
DR EMBL; QOCS01000005; RHW48439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347SU98; -.
DR KEGG; lbm:DS830_01730; -.
DR Proteomes; UP000261753; Chromosome.
DR Proteomes; UP000284822; Unassembled WGS sequence.
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; 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}.
FT DOMAIN 1..82
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 447..561
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 120..130
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 561 AA; 63430 MW; 4FD12935BFFE6770 CRC64;
MQQTLSAGLL TLGDLNLSET QIAQMIEVPK DSKMGDFAFP TFQLAKQLHQ APVQIAQNLV
KQLDTSAFAQ VQAQGPYVNF FLQRNSIAKT TITQVIEQGS DFGNHTIGQQ ANVVIDMSSP
NIAKPMSMGH LRSTVIGNSI ALILNKLGYQ PVKINHLGDW GTQFGKLMVA YKKWGSEEEV
KQDPITNLQK YYVKFHQLDK EHPELDDEAR EWFKKLENGD EEATYLWKWF RSESLKAFMK
VYDELGISFD SYNGEAFYND KMDEVVDLLA QKGLLQESQG AEIVDLGPDL PPALIKKSDG
ATLYITRDLA AALYRQRTYH FKKALYVVGS EQSVHFEQLK AVLAKMGYDW AQDIEHIKFG
LITSEGKKLS TRAGRVILLE NVLHDSVKLA RNQIDEKNPT LANKEEVAHE VGVGAVIFHD
LKNNRTDNFD FNLDEVVRFE GETGPYVQYT HARAMSILRK ADYQETKTDI TPDQIDDQTW
EILKFLANFP NIIQQAALQR EPSVIAKYAL RLAKAFNHYY AHTKVLVADE QLSTRLALVK
AVTIVLKESL RLLGVQAPDE M
//