ID SYR_HAEIG Reviewed; 577 AA.
AC A5UJ40;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 01-MAY-2013, entry version 42.
DE RecName: Full=Arginine--tRNA ligase;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=argS; OrderedLocusNames=CGSHiGG_10215;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R.,
RA Post J.C., Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12
RT clinical nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC diphosphate + L-arginyl-tRNA(Arg).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
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DR EMBL; CP000672; ABR00796.1; -; Genomic_DNA.
DR RefSeq; YP_001293179.1; NC_009567.1.
DR ProteinModelPortal; A5UJ40; -.
DR STRING; 374931.CGSHiGG_10215; -.
DR PRIDE; A5UJ40; -.
DR EnsemblBacteria; ABR00796; ABR00796; CGSHiGG_10215.
DR GeneID; 5227846; -.
DR KEGG; hiq:CGSHiGG_10215; -.
DR PATRIC; 20188450; VBIHaeInf102487_2063.
DR eggNOG; COG0018; -.
DR HOGENOM; HOG000247212; -.
DR KO; K01887; -.
DR OMA; QGAKCVF; -.
DR ProtClustDB; PRK01611; -.
DR BioCyc; HINF374931:GJA4-1764-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:HAMAP.
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_Ia.
DR InterPro; IPR015945; Arg-tRNA-synth_Ia_core.
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_1a_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; SSF55190; Arg-tRNA-synth_Ic_N; 1.
DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 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 1 577 Arginine--tRNA ligase.
FT /FTId=PRO_1000018036.
FT MOTIF 122 132 "HIGH" region.
SQ SEQUENCE 577 AA; 64785 MW; B621B28DE09D35A6 CRC64;
MNIQSILSDK IKQAMILAGA DQSCDALIRQ SGKPQFGDYQ ANGIMAAAKK LGLNPREFAQ
KVLDNAQLSD IAEKLEIAGP GFINIFLNPT WLTTEISAAL SHKNLGIQAT NKQTVVIDYS
SPNVAKEMHV GHLRSTIIGD AVARTLEFLG HNVIRANHVG DWGTQFGMLI AYLEKMQHEH
ASEMELQDLE AFYREAKKHY DEDEIFAEKA RNYVVKLQSG DEYCRTMWKR LVDITMQQNQ
HNYNRLNVTL TEKDVMGESL YNPMLPSIVE DLKKQGLAVE NDGALVVYLD EFKNKDGDPM
GVIVQKKDGG FLYTTTDIAA AKYRYETLKA NRALVFSDTR QSQHMQQAWL ITRKAGYVPD
SFSLEHKNFG MMLGKDGKPF KTRTGGTIKL ADLLDEAIER ATVLINEKNT NLSNDEKEAV
IEAVGIGAVK YADLSKNRTT DYVFDWDNML SFEGNTAPYM QYAYTRIRSI FNKTDINSTA
LLAAPLTIKD DKERTLAIKL LQFEEAVQTV GKEGTPHVLC AYLYELAGIF SSFYEHCPIL
NAEDESIKLS RLKLALLTEK TLKQGLTLLG IKTVEKM
//
