ID SYR_SYNAS Reviewed; 562 AA.
AC Q2LVV5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 29-MAY-2013, entry version 50.
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=SYNAS_23320; ORFNames=SYN_00994;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophaceae; Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RA Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A.,
RA Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.;
RT "The genome of the syntrophic bacterium Syntrophus aciditrophicus:
RT Life dependent on negative change in electrical potential.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000252; ABC78211.1; -; Genomic_DNA.
DR RefSeq; YP_462379.1; NC_007759.1.
DR ProteinModelPortal; Q2LVV5; -.
DR STRING; 56780.SYN_00994; -.
DR GeneID; 3883282; -.
DR KEGG; sat:SYN_00994; -.
DR PATRIC; 23865472; VBISynAci70500_2518.
DR eggNOG; COG0018; -.
DR HOGENOM; HOG000247214; -.
DR KO; K01887; -.
DR OMA; HTSANPN; -.
DR ProtClustDB; PRK01611; -.
DR BioCyc; SACI56780:GHXT-2381-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 1 562 Arginine--tRNA ligase.
FT /FTId=PRO_0000242109.
FT MOTIF 137 147 "HIGH" region.
SQ SEQUENCE 562 AA; 63784 MW; CF79779665CAC2DB CRC64;
MQIMIGSSIK HRLTMLVKNA VDGCVAEGLL AGGNFPPVEM EMTKDTVHGD YATNFAMVMA
SHARMNPRKI AEMISSHFRD GEQILEKTEI AGPGFINFFV RENVWAEQLK DIESLGNHYG
SAETGRGKKV QVEFVSANPT GPLHIGHARG AVVGDVIANI LGMSGYEIFR EYYINDAGNQ
MNNLGKSVWY RYQELLGRSV EFPDTCYQGD YIREIAGDIL KKDGDIHLTS NEDSNIRFFT
DYAAGIILEE IKQDLKDFGI VFDKYFSERE LYVNDGVARL LADLEEKGFI YRDDETLWFK
TTDFGDDKDR VVVRKNGEPT YFAADIAYHK NKYERGFDSV IDIWGADHHG YIPRMHAGIQ
ALGHSKDALR VVLVQLVNLL RDGKPVAMST RSGEFVTMKE VVDEVGRDAA RYNFLMRRSD
SHLDFDLEVA KRQSNENPVY YVQYAHARIC SILRMAKERG IELPSFENVE PQLLRIPEEI
ALIKTLTRFP EVVEGSARTL EPHRITFYLN DLAGLFHSYY NKYKVISDDE AMTRTRLFLV
KCIQTVLKNA LTLLGVSAPE KM
//
