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Database: UniProt
Entry: A0A347SU98_9LACO
LinkDB: A0A347SU98_9LACO
Original site: A0A347SU98_9LACO 
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
//
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