ID K0AGZ7_EXIAB Unreviewed; 560 AA.
AC K0AGZ7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123,
GN ECO:0000313|EMBL:AFS71756.1};
GN OrderedLocusNames=Eab7_2671 {ECO:0000313|EMBL:AFS71756.1};
OS Exiguobacterium antarcticum (strain B7).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1087448 {ECO:0000313|EMBL:AFS71756.1, ECO:0000313|Proteomes:UP000006274};
RN [1] {ECO:0000313|EMBL:AFS71756.1, ECO:0000313|Proteomes:UP000006274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|Proteomes:UP000006274};
RX PubMed=23144424; DOI=10.1128/JB.01791-12;
RA Carneiro A.R., Ramos R.T., Dall'Agnol H., Pinto A.C., de Castro Soares S.,
RA Santos A.R., Guimaraes L.C., Almeida S.S., Barauna R.A., das Gracas D.A.,
RA Franco L.C., Ali A., Hassan S.S., Nunes C.I., Barbosa M.S., Fiaux K.K.,
RA Aburjaile F.F., Barbosa E.G., Bakhtiar S.M., Vilela D., Nobrega F.,
RA Dos Santos A.L., Carepo M.S., Azevedo V., Schneider M.P., Pellizari V.H.,
RA Silva A.;
RT "Genome sequence of Exiguobacterium antarcticum B7, isolated from a biofilm
RT in Ginger Lake, King George Island, Antarctica.";
RL J. Bacteriol. 194:6689-6690(2012).
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:0000256|ARBA:ARBA00001766,
CC ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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DR EMBL; CP003063; AFS71756.1; -; Genomic_DNA.
DR RefSeq; WP_014971572.1; NC_018665.1.
DR AlphaFoldDB; K0AGZ7; -.
DR STRING; 1087448.Eab7_2671; -.
DR KEGG; ean:Eab7_2671; -.
DR PATRIC; fig|1087448.3.peg.2740; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_9; -.
DR Proteomes; UP000006274; 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; cd07956; Anticodon_Ia_Arg; 1.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
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 NCBIfam; TIGR00456; argS; 1.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}.
FT DOMAIN 5..84
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 449..560
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 121..131
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 560 AA; 63226 MW; B861A65385E651F8 CRC64;
MSYKQQYAKV LHDVIGDALS QEEIEQLIEQ PKHEDHGDLA FPCFQLAKAF RKAPMMIATE
LAEKIDNPLF SNVQAAGPYV NVFLNREIVS REIVKRVLEE KQAYGSSEPT GKTIVTDFSS
PNIAKPFSMG HLRSTVIGNA LNQISRKKGY DVVGINHLGD WGTQFGKLMV AYNMWGKEED
VRAEPIKELL KLYVRFHEEA EENPALEDEG RAWFKKLEQG DEQATALWTW FREVSLVEFN
RVYQMLGVSF DSLNGEAFYN DKMQHVIDLL EEKELLVESE GAMVVDLEAE GMPPALIKKK
DGATLYATRD LAAAVYRLET YGFEQAFYVV GGEQALHFKQ LFAVLKKLGF ENVDGMHHVP
FGLIMKDGKK MSTRKGRIVL LEEVLQDAIN VAKQNIAEKN PNLANAEQTA REVGVGAVIF
HDLKNERMNN IEFDLEQMLK FEGETGPYVQ YTNARANSLL RKGEYDGSAF VGSADDYSWG
VVSMLNQFST VIDRAFTRRE PSIISRYVLD LAQSFNKYYG QVRVLEEDAE KQSRLALVKS
VTIVLTEGLR LLGVGAPEEM
//
