ID A0A1B3SJQ9_9MOLU Unreviewed; 553 AA.
AC A0A1B3SJQ9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:AOG60158.1};
GN ORFNames=SHELI_v1c02030 {ECO:0000313|EMBL:AOG60158.1};
OS Spiroplasma helicoides.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=216938 {ECO:0000313|EMBL:AOG60158.1, ECO:0000313|Proteomes:UP000094378};
RN [1] {ECO:0000313|EMBL:AOG60158.1, ECO:0000313|Proteomes:UP000094378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TABS-2 {ECO:0000313|EMBL:AOG60158.1,
RC ECO:0000313|Proteomes:UP000094378};
RA Shen W.-Y., Lo W.-S., Lai Y.-C., Kuo C.-H.;
RT "Complete genome sequence of Spiroplasma helicoides TABS-2 (DSM 22551).";
RL Submitted (AUG-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; CP017015; AOG60158.1; -; Genomic_DNA.
DR RefSeq; WP_069115933.1; NZ_CP017015.1.
DR AlphaFoldDB; A0A1B3SJQ9; -.
DR STRING; 216938.SHELI_v1c02030; -.
DR KEGG; shj:SHELI_v1c02030; -.
DR PATRIC; fig|216938.3.peg.203; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000094378; 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:UP000094378}.
FT DOMAIN 2..86
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 435..553
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 122..132
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 553 AA; 63619 MW; A64B4555F343650F CRC64;
MSIFIEKINN AFENILKKSN LQGRIIIEKP REESNGDFST NFAMINSKLN NMKPLDLASQ
LVKSLNETNL FEKVEIAGPG FINMTMKNDF LKDVLNKIIK EKDHYGSSDK KDFKYNIEIV
SANPTGYLHI GHARNGSIGD SVARMLKFLG YQVETEHYTN DAGNQINISA STLFYQYLKL
LNIEVQPPEE MYGGDMYVEV AKLFLDKYGD KFKDNRLNGN IIDDEEVHKI FRKESISFFL
EIIKNQLKML GVQIDLFSSE AQIYAQNEVE KTLSLYENLG KTYWKDDALW IKTTELGDDK
DRVLKKANGE FTYISGDLAS HNVRFQRSNA NKYVNFWGAD HHGYIPRIKA GLTLLGYPKD
ILEIDIYQMV RVIKDGQEVK MSKRRGTAIW LIDLIEMVGK DSTRYMLVSK PPTSHMDFDL
DLVMSKNSAN PVYYAQYATA RAFKILEKAQ EHGLTLNNTN FNLLDNEKEK QIIMLLDSFN
KTIEYAATSR LPSVVCDYIQ NLAKKFHSYY SEFKFFDEQN KELSTQRCIL VEAIYQVLSN
AFNLIGIDVV NEM
//
