SYR1_ALKHC
ID SYR1_ALKHC Reviewed; 556 AA.
AC Q9K6C1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Arginine--tRNA ligase 1;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase 1;
DE Short=ArgRS 1;
GN Name=argS1; OrderedLocusNames=BH3808;
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; BAB07527.1; -; Genomic_DNA.
DR PIR; H84125; H84125.
DR RefSeq; WP_010899933.1; NC_002570.2.
DR AlphaFoldDB; Q9K6C1; -.
DR SMR; Q9K6C1; -.
DR STRING; 272558.10176433; -.
DR EnsemblBacteria; BAB07527; BAB07527; BAB07527.
DR KEGG; bha:BH3808; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_9; -.
DR OMA; YEFKWER; -.
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; 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 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..556
FT /note="Arginine--tRNA ligase 1"
FT /id="PRO_0000151528"
FT MOTIF 132..142
FT /note="'HIGH' region"
SQ SEQUENCE 556 AA; 62870 MW; 44FEBEE7FE345ED8 CRC64;
MNKMEQMKQQ LREEIVVAVK AAGLATDETI PEVILETPKE KAHGDFATNM AMQLARVAKK
APRLIAEELT AKLDRKRAAI EKIEIAGPGF INFFLDNSYL REMIPTVLRA ESAYGETNVG
KGKKVQVEFV SANPTGNLHL GHARGAAVGD ALCNILAKAG YDVSREYYIN DAGNQINNLA
LSLEARYFQA LGMEKDMPED GYHGEDIIQF GKDLAETHGD KFVHESSEER LAFFREYGLK
RELEKIKSDL EEFRVPFDNW YSETSLYTTG KVEKTLNVLK EKGKTYEQDG ALWFRSTEYG
DDKDRVLVKN DGSYTYLTPD ISYHEDKFLR GFEKLINIWG ADHHGYIPRM KAAIQALGYE
KDQLDVQIIQ MVSLFQNGEK VKMSKRTGKA VTLRDLMEEV GIDATRYFFA MRSADSHLDF
DMDLAVSKSN ENPVYYVQYA HARVCSMLRK GKELGLSFDE STDLSPIASE KEYDLLKKIG
EFPEVVAEAA QKQMPHRITN YVHELASTLH SFYNAEQVIN PENDEQSKAR LALMKATQVT
LKNALSLVGV EAPERM