SYR2_ALKHC
ID SYR2_ALKHC Reviewed; 561 AA.
AC Q9KEL8;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Arginine--tRNA ligase 2;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase 2;
DE Short=ArgRS 2;
GN Name=argS2; OrderedLocusNames=BH0834;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BA000004; BAB04553.1; -; Genomic_DNA.
DR PIR; B83754; B83754.
DR RefSeq; WP_010897007.1; NC_002570.2.
DR AlphaFoldDB; Q9KEL8; -.
DR SMR; Q9KEL8; -.
DR STRING; 272558.10173449; -.
DR PRIDE; Q9KEL8; -.
DR EnsemblBacteria; BAB04553; BAB04553; BAB04553.
DR KEGG; bha:BH0834; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_9; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001258; 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; -; 1.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR11956; PTHR11956; 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; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..561
FT /note="Arginine--tRNA ligase 2"
FT /id="PRO_0000151529"
FT MOTIF 117..127
FT /note="'HIGH' region"
SQ SEQUENCE 561 AA; 64133 MW; C9C544BF1DE1A1FF CRC64;
MLAQMISEEL ARILSLKEDE VERLLEIPPQ ETLGDLAFPC FTLAKTKRKA PPFIAAELEA
AFLEHKEVTA KATGGYVNFF FHRETVAGQL FQEMKSNQYW QPNSGDGKRV VIDMSSPNIA
KPFGIGHLRS TIIGHALYHL LKKTGYDPIR VNHLGDWGTQ FGKQIAAYQR WGGDVDLKQN
PIASFLELYV RFHEEAEKDE SLEDEGREWF KKLEEGDEEA DRLWTYFVKE SLNEFDRMYN
RLGVEFDYVL GESFYNDQMA PVVKELQEKG LLTCSEGALV VPLEDADLPP CLIVKSDGTS
IYATRDLATA IYRHHVQKGE KLLYVVGGEQ TLHFKQVFHV LKKMGYKWAD QCEHITFGLL
RLDGKKMSTR RGRVVMLEDV LNDVVAHAKA KIKEKHPNHP HLHEVAEAVG VGAVIFGDLK
QDRRLDVNFR LEDALSFEGE TGPYVQYTYA RIQSILRKGD KLNDSRHMDW QHVTKDEGWS
LLKVLIQYPN VLIKATEARE PHQLARYVLT VSKKFNQFYH KYVILADDET VRQARLILAE
RTGEVIADAM AVLGVKTPEE L