ID SYR_LISW6 Reviewed; 556 AA.
AC A0ALP7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 01-MAY-2013, entry version 46.
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=lwe2511;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 /
OS SLCC5334).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / SLCC5334;
RX PubMed=16936040; DOI=10.1128/JB.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R.,
RA Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T.,
RA Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J.,
RA Liang C., Dandekar T., Lampidis R., Kreft J., Goebel W.,
RA Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK21929.1; -; Genomic_DNA.
DR RefSeq; YP_850708.1; NC_008555.1.
DR ProteinModelPortal; A0ALP7; -.
DR STRING; 386043.lwe2511; -.
DR EnsemblBacteria; CAK21929; CAK21929; lwe2511.
DR GeneID; 4464970; -.
DR KEGG; lwe:lwe2511; -.
DR PATRIC; 20332279; VBILisWel39304_2520.
DR eggNOG; COG0018; -.
DR HOGENOM; HOG000247214; -.
DR KO; K01887; -.
DR OMA; HTSANPN; -.
DR ProtClustDB; PRK01611; -.
DR BioCyc; LWEL386043:GI5X-2530-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 1 556 Arginine--tRNA ligase.
FT /FTId=PRO_1000018054.
FT MOTIF 132 142 "HIGH" region.
SQ SEQUENCE 556 AA; 62818 MW; C53AF1F179D727DD CRC64;
MNVMQENQIK LIEHIKQAVV QAVGLPEVEV PEILLEVPKD KKHGDYSTNI AMQLARVAKK
APRQIAESIV PELKKDNKLI KEVEIAGPGF INFYLDNAYL TELVPVILTE DHKYGESDFG
KGEKFQIEFV SANPTGDLHL GHARGAAIGD SLANIMKMAG FDVSREYYIN DAGNQINNLV
LSAEARYFEA LGLESEFPED GYRGADIISL GKDLAAKYGD KYVNTSEEER RSVFRVDALA
FETGKLRADL EEFRVSFDEW FSETSLYEEN KVLPALERLR ENGYIYEQDG ATWLRTTDFE
DDKDRVLIKS DGSYTYFLPD IAYHLNKLER GFDVLIDIWG ADHHGYIPRM RAAIEALGYS
PNQLEVEIIQ LVHLFEDGVQ VKMSKRTGKS VTMRDLIEEV GLDATRYFFA MRSSDTHMNF
DMSLAKSTSN DNPVYYVQYA HARISSILRS GKEQGLEVTK DADMSLLQTE AEYDLLKVLG
EFADVVAEAA AKRAPHRIVR YLNDLATAFH RFYNSNKVLD MDNLEVTQAR LSLIKTAQIT
LRNGLTLLGV SAPEKM
//
