ID I3EBP1_BACMM Unreviewed; 556 AA.
AC I3EBP1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:AIE61593.1};
GN ORFNames=BMMGA3_16200 {ECO:0000313|EMBL:AIE61593.1};
OS Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE61593.1, ECO:0000313|Proteomes:UP000027602};
RN [1] {ECO:0000313|EMBL:AIE61593.1, ECO:0000313|Proteomes:UP000027602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGA3 / ATCC 53907 {ECO:0000313|Proteomes:UP000027602};
RX PubMed=25758049;
RA Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT previously uncharted transcriptional landscape.";
RL BMC Genomics 16:73-73(2015).
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; CP007739; AIE61593.1; -; Genomic_DNA.
DR RefSeq; WP_003346880.1; NZ_CP007739.1.
DR AlphaFoldDB; I3EBP1; -.
DR STRING; 796606.BMMGA3_16200; -.
DR KEGG; bmet:BMMGA3_16200; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_9; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000027602; 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; 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:UP000027602}.
FT DOMAIN 5..95
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 437..556
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 132..142
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 556 AA; 62983 MW; 1203562578F48525 CRC64;
MNIVEQVQNK LKEEIKAAVL KANLAAVEEI PDVILEVPKE KSHGDYSTNM AMQLARVAKK
APRMIAEELV AHFDRSKASI EKIEIAGPGF INFYMNNSYL TDLIPTILDK GDAYGETTVG
GNQKVLVEFV SANPTGDLHL GHARGAAVGD SLCNILDKAG FNVSREYYIN DAGNQINNLA
RSVEARYFQA LGIEKEMPED GYYGEDIVEI GKKLAEEFGD KYVNADEKER FNFFREYGLK
YEMEKLKKDL ENFRVKFDVW YSETSLYHNG KIDEALQALK DNGHIYEQDG ATWFRSTEFG
DDKDRVLIKQ DGSYTYLTPD IAYHKDKLER GFEKLINIWG ADHHGYIPRM KAAIEALGYD
RDVLEVEIIQ LVHLYKNGEK MKMSKRTGKA VTMRELVEEV GLDAVRYFFA MRSSDTHMDF
DLDLAVSQSN ENPVYYAQYA HARICSILRQ GEEQGLTFDR NADFSVIQSE KETDLLKKLG
EFPQAVGEAA QKRMPHRITN YIFDLASAFH SFYNAEKVLD PENEATTKAR LALVKAVQIT
LKNALALIGV SAPEKM
//
