SYR_VIBPA
ID SYR_VIBPA Reviewed; 577 AA.
AC Q87RD6;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=VP0861;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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}.
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DR EMBL; BA000031; BAC59124.1; -; Genomic_DNA.
DR RefSeq; NP_797240.1; NC_004603.1.
DR RefSeq; WP_005455463.1; NC_004603.1.
DR AlphaFoldDB; Q87RD6; -.
DR SMR; Q87RD6; -.
DR STRING; 223926.28805847; -.
DR DNASU; 1188358; -.
DR EnsemblBacteria; BAC59124; BAC59124; BAC59124.
DR GeneID; 1188358; -.
DR KEGG; vpa:VP0861; -.
DR PATRIC; fig|223926.6.peg.815; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002493; Chromosome 1.
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..577
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151633"
FT MOTIF 122..132
FT /note="'HIGH' region"
SQ SEQUENCE 577 AA; 63871 MW; 8BF8273F071A48D2 CRC64;
MNIQALINDK VSQALEAAGA PAGSPAAVRQ SAKPQFGDYQ ANGVMGVAKK LGTNPREFAQ
KVLDVLDLDG IASKTEIAGP GFINIFLSEE FLAKQADAAL ADSRLGVAAE EAQTIVADYS
APNVAKEMHV GHLRSTIIGD AVVRTLEFLG HKVIRANHIG DWGTQFGMLI ANLERVQQES
GEVSMELADL EGFYRESKKL YDEDEEFAVK ARNYVVKLQS GDEFCAEMWK KLVDVTMIQN
QRNYDRLNVS LTRDDVMGES MYNDMLPKIV ADLKAQGLAV EDDGAQVVFL EEFKNKDGEA
MGVIVQKRDG GFLYTTTDIA CAKYRYEELG ADRVLYFIDS RQHQHLMQAW TIVRKAGYVP
ESVSLEHHAF GMMLGKDGKP FKTRAGGTVR LADLLDEAEV RAAQLIESKN PELDAEEKEK
ISKTVAMAAV KYSDLSKHRT TDYVFDWDNM LAFEGNTAPY MQYAYTRVAS IFAKAGVAMD
ELQGDIQITD EKEKALIAKL LQFEEAVQSV AREGQPHIMC SYLFELAGQF SSFYEACPIL
VAEDEAVKQS RLKLAALTAK TIKQGLSLLG IETLERM
