SYR_HAEIG
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 25-MAY-2022, entry version 76.
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=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., Post J.C.,
RA 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 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABR00796.1; -; Genomic_DNA.
DR RefSeq; WP_012055504.1; NC_009567.1.
DR AlphaFoldDB; A5UJ40; -.
DR SMR; A5UJ40; -.
DR EnsemblBacteria; ABR00796; ABR00796; CGSHiGG_10215.
DR KEGG; hiq:CGSHiGG_10215; -.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000001990; 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.
FT CHAIN 1..577
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018036"
FT MOTIF 122..132
FT /note="'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