(data stored in ACNUC7421 zone)

SWISSPROT: SYR_SHESH

ID   SYR_SHESH               Reviewed;         581 AA.
AC   A8FQM2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 60.
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};
GN   OrderedLocusNames=Ssed_0533;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg). {ECO:0000255|HAMAP-
CC       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
CC       family. {ECO:0000255|HAMAP-Rule:MF_00123}.
DR   EMBL; CP000821; ABV35145.1; -; Genomic_DNA.
DR   RefSeq; WP_012140882.1; NC_009831.1.
DR   ProteinModelPortal; A8FQM2; -.
DR   STRING; 425104.Ssed_0533; -.
DR   EnsemblBacteria; ABV35145; ABV35145; Ssed_0533.
DR   KEGG; sse:Ssed_0533; -.
DR   eggNOG; ENOG4105C75; Bacteria.
DR   eggNOG; COG0018; LUCA.
DR   HOGENOM; HOG000247212; -.
DR   KO; K01887; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; POG091H01RF; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 1.10.730.10; -; 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; 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;
DR   PRODOM; A8FQM2.
DR   SWISS-2DPAGE; A8FQM2.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    581       Arginine--tRNA ligase.
FT                                /FTId=PRO_1000076232.
FT   MOTIF       126    136       "HIGH" region.
SQ   SEQUENCE   581 AA;  65066 MW;  0EA349F8DCC74CDC CRC64;
     MKSHIQSLLI QALDALKQQG VIPTDFEARV QVDRTKDKTH GDFATNLAMM LTKVARKNPR
     ELAQLIIDSL PQDSQVAKVE IAGPGFINFF IDENALASQL MAALNDDHLG IQLPEPQTVV
     VDYSSPNLAK EMHVGHLRST IIGDSVVRAL EFQGHNVIRQ NHVGDWGTQF GMLLAYMEEL
     RAENGEQAQM ELSDLETFYR AAKVRFDESE DFAIRARKLV VSLQSGDEYC NKLWREFNDI
     SLSHCHDVYE RLGVSLTRKD VRGESTYNDD LEQVVKDLDA KGLLSESNGA KVVFQDEFKT
     KDGDPLPVII QKADGGYLYA TSDLAAMRYR SNVLKADRAL YFVDLRQGLH FQQVFKLART
     AEFINPDMSL EHMGFGTMNG DDGRPFKTRS GGVVKLVDLL TEADTRALEL VRSKNPDMDQ
     AELEKIAKVV GISSVKYADL SKNRASDYIF SFEQMLSFEG NTAPYLLYAY TRVAGIFKRA
     TDIDLSDAKM QLDHDKEKDL GNKLAQFGEV LSRMVTKGQP HALCGYLFEL AGAFSSFYEA
     CPVLAAESEE QKKSRLLLSQ LTAKTLKQGL DLLGIETLER M
//

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