SYR_BORPE
ID SYR_BORPE Reviewed; 560 AA.
AC Q7W0K0;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=BP0115;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE40495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX640411; CAE40495.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_879017.1; NC_002929.2.
DR RefSeq; WP_023853376.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7W0K0; -.
DR SMR; Q7W0K0; -.
DR STRING; 257313.BP0115; -.
DR GeneID; 45390601; -.
DR KEGG; bpe:BP0115; -.
DR PATRIC; fig|257313.5.peg.117; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_4; -.
DR Proteomes; UP000002676; 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..560
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151536"
FT MOTIF 164..174
FT /note="'HIGH' region"
SQ SEQUENCE 560 AA; 61387 MW; FF6C5F443BB1EB2E CRC64;
MLLEQQKQLI SLIQAAVAQC LPEAQAQVQL ERPKVAAHGD IATNVAMQLA KPARRNPREL
AQGIVDALMA QPQARELIQD AEIAGPGFIN FRLTPAARQA VVQAVASQAD AYGRAPRNGE
KVLVEFVSAN PTGPLHVGHA RQAALGDAIC RLYDASGWDV TREFYYNDAG NQIDNLAISV
QARGRGIAPD APDYPADGYK GDYIVEIARD FAARKSVQAS DGQPVTATGD LDSLDDIRAF
AVAYLRREQD LDLQAFGLAF DNYFLESSLY ASGRVQETVD TLVAKGHTYE EGGALWLRTT
ELGTGDDKDR VMRKSEGGYT YFVPDVAYHK VKWERGFHHA VNIQGSDHHG TVARVRAGLQ
GLAGIPKDFP AYVLHKMVKV MRGGEEVKIS KRAGSYVTMR DLIDWVGRDA VRYFLIQRRA
DTEFVFDIDL ALSKSDENPV YYIQYAHARI CTMIGNSGAS AAEIAQADTA LLTAPSEYAL
LQRLAEFPQV VALAAQELAP HHVAFWLRDC ASDFHAWYNA ERVLVDEPAL KLARLRLAAT
TRQVLANGLA LLGVSAPDRM