ID M4SDX0_9SPHN Unreviewed; 575 AA.
AC M4SDX0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:AGH48827.1};
GN ORFNames=G432_05500 {ECO:0000313|EMBL:AGH48827.1};
OS Sphingomonas sp. MM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH48827.1, ECO:0000313|Proteomes:UP000011816};
RN [1] {ECO:0000313|EMBL:AGH48827.1, ECO:0000313|Proteomes:UP000011816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH48827.1};
RX PubMed=23682148;
RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT Bacterium Sphingomonas sp. Strain MM-1.";
RL Genome Announc. 1:E00247-13(2013).
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; CP004036; AGH48827.1; -; Genomic_DNA.
DR RefSeq; WP_015457842.1; NC_020561.1.
DR AlphaFoldDB; M4SDX0; -.
DR STRING; 745310.G432_05500; -.
DR KEGG; sphm:G432_05500; -.
DR PATRIC; fig|745310.14.peg.1138; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_5; -.
DR Proteomes; UP000011816; 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:UP000011816}.
FT DOMAIN 5..94
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 451..574
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 131..141
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 575 AA; 62387 MW; 249FBDFAD9A2B6D7 CRC64;
MTLYARFADR IGQILDDLAQ AGDLPAGLDR RNVTVEPPRD PAHGDLATNA AMVLAKPAGK
NPRELASLIA PKLARLPEIA SAEVAGPGFI NVRLTEESWR EELAAILAGG ADYGRSTIGK
GERVNVEYVS ANPTGPMHMG HCRGAVVGDA LASLLEYAGY AVTREYYIND AGSQVETLAR
SAHLRYRQAL GEQGITIPEG LYPGDYLIPI GEKLATEFGD RYARAPEGEW LVLFREKTVA
AMMDLIRADL ALLGIHHDVF ASEAKVQKDG RVKAALDKLR AEGLVYEGVL EAPKGEVPED
WEPVEMTLFR ATAFGDDSDR PVMKADGSLT YFGTDLAYHA QKAETADQLI DIWGADHAGT
VKRIQAAVKA LTGGKVPLDI KLVQMVRLLR GGEPVKMSKR SGSFVTLADV VREVGKDVVR
FTMLTRKADA QMDFDFAKVV EASKDNPVFY VQYAHARVHS LHRRLAEAGL ALPAADLGRL
DGEELALVKL AAQFPRLIEG AAANHEPHRV AFYLYDLAAA FHALWNRGND DPSRRFLLVD
DAETTAARLA LADAIGQIIR NGLAVMGVAA AEEMH
//
