ID SYR_PSEA7 Reviewed; 587 AA.
AC A6VDH2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 02-NOV-2016, 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=PSPA7_5788;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-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; CP000744; ABR86159.1; -; Genomic_DNA.
DR RefSeq; WP_003156914.1; NC_009656.1.
DR ProteinModelPortal; A6VDH2; -.
DR PRIDE; A6VDH2; -.
DR EnsemblBacteria; ABR86159; ABR86159; PSPA7_5788.
DR KEGG; pap:PSPA7_5788; -.
DR PATRIC; 19833061; VBIPseAer80442_5506.
DR HOGENOM; HOG000247212; -.
DR KO; K01887; -.
DR OMA; KLVGNYY; -.
DR Proteomes; UP000001582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
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; 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; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1 587 Arginine--tRNA ligase.
FT /FTId=PRO_1000018090.
FT MOTIF 127 137 "HIGH" region.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 127 138 ipat:AA_TRNA_LIGASE_I [T]
FT MYHIT 101 457 ipfam:tRNA-synt_1d [T]
FT MYHIT 471 587 ismart:DALR_1 [T]
FT MYHIT 4 90 ipfam:Arg_tRNA_synt_N [T]
FT MYHIT 471 587 ipfam:DALR_1 [T]
FT MYHIT 3 587 ihamap:Arg_tRNA_synth [T]
FT MYHIT 3 91 ismart:Arg_tRNA_synt_N [T]
SQ SEQUENCE 587 AA; 65353 MW; A845D5C81688EA97 CRC64;
MKDTIRQLIQ QALDQLTADG TLPAGLTPDI QVENTKDRSH GDFASNIAMM LAKPAGMKPR
DLATRLVEAL PAHEQLAKVE IAGPGFLNFF QDHIWLAASL DRALADERLG VRKAGPAQRV
VIDLSSPNLA KEMHVGHLRS TIIGDAVARV LEFLGDTVIR QNHVGDWGTQ FGMLLAYLEE
QPVDAQAELH DLEVFYRAAK KRFDESPEFA DRARELVVRL QAGDPDCLRL WTRFNEISLS
HCQKVYDRLG VKLSMADVKG ESAYNDDLAQ VVADLTAKGL LTEDNGALCV FLEEFRNAEG
NPLPVIVQKA GGGYLYATTD LAAMRYRHNV LHADRALYFV DQRQALHFQQ VFEVARRAGF
VPADMELEHM GFGTMNGADG RPFKTRDGGT VKLIDLLEEA ESRAYALVKE RNEQRVERGE
EPFDEAQLRE IGRVVGIDSV KYADLSKHRT SDYSFNFELM LSFEGNTAPY LLYACTRVAS
VFRKLGQGRE QLGGRIVLEQ PQELALAAQL AQFGDLLNNV ALKGVPHLLC AYLYELAGLF
SSFYEHCPIL TAEDPAQKDS RLRLAALTGR TLEQGLELLG LKTLERM
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