SYR1_BACAN
ID SYR1_BACAN Reviewed; 556 AA.
AC Q81JT7; Q6HQD6; Q6KJR4;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Arginine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS 1 {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS1 {ECO:0000255|HAMAP-Rule:MF_00123};
GN OrderedLocusNames=BA_5611, GBAA_5611, BAS5213;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; AE016879; AAP29249.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34757.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57502.1; -; Genomic_DNA.
DR RefSeq; NP_847763.1; NC_003997.3.
DR RefSeq; WP_001086469.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_031452.1; NC_005945.1.
DR AlphaFoldDB; Q81JT7; -.
DR SMR; Q81JT7; -.
DR IntAct; Q81JT7; 7.
DR STRING; 260799.BAS5213; -.
DR DNASU; 1085315; -.
DR EnsemblBacteria; AAP29249; AAP29249; BA_5611.
DR EnsemblBacteria; AAT34757; AAT34757; GBAA_5611.
DR GeneID; 45025192; -.
DR KEGG; ban:BA_5611; -.
DR KEGG; bar:GBAA_5611; -.
DR KEGG; bat:BAS5213; -.
DR PATRIC; fig|198094.11.peg.5569; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_9; -.
DR OMA; YEFKWER; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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_0000151525"
FT MOTIF 132..142
FT /note="'HIGH' region"
SQ SEQUENCE 556 AA; 62490 MW; 33A24EF2711A5594 CRC64;
MNSLEQVKGL IKEEIQAAVL KAELATEEQI PNVVLESPKD KTNGDFSTNM AMQLARVAKK
APRMIAEELV ANFDKAKAST EKIEIAGPGF INFYMDNSYL TDLIPTIVNA GEAYGETNTG
KGEKVQVEFV SANPTGDLHL GHARGAAVGD TLCNLLAKAG YDVSREYYIN DAGNQIHNLA
LSVEARYMQA LGLEKEMPED GYHGADIIGI GKRLAEEFGD RYAKADEKES YEFYREYGLK
YELAKLQKDL ESFRVKFDVW FSETSLYKNG KIDQALAVLK ERDEIFEEDG ATWFRSMTYG
DDKNRVLIKN DGSYTYLTPD IAYHRDKLER GFDKLINIWG ADHHGYIPRM KAAIQALGYD
KETLEVEIIQ MVQLYQNGEK MKMSKRTGKA VTLRELMEEV GVDAMRYFFA MRSGDSHLDF
DMDLAVSKSN ENPVYYAQYA HARVCSILRQ GEELGLATGG DVNYKLVTSE KEVELLKKLG
EFPAVVADAA QKRLPHRITN YAFELAATLH SFYNAEKVLN QDNLELSKAR YELMKAVRTT
LQNALAIVGV SAPEKM
