SYR_TRIV2
ID SYR_TRIV2 Reviewed; 588 AA.
AC Q3M769;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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}; OrderedLocusNames=Ava_3561;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA23167.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3M769; -.
DR SMR; Q3M769; -.
DR STRING; 240292.Ava_3561; -.
DR EnsemblBacteria; ABA23167; ABA23167; Ava_3561.
DR KEGG; ava:Ava_3561; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_3; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002533; 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..588
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000241974"
FT MOTIF 126..136
FT /note="'HIGH' region"
SQ SEQUENCE 588 AA; 65554 MW; 5CB9FB06D47521AD CRC64;
MNATQEQLKV KLEQALIAAF GDEYAGVDPI LVTASNPKFG DYQANVALSL SKKLGQPPRA
IASAIVEKLD VSEICETPEI AGPGFINLKL KTAYLEAQLN AIQADSRLGV PTAKHPQREI
VDFSSPNIAK EMHVGHLRST IIGDSIARIL EFRGHDVLRL NHVGDWGTQF GMLITYLREV
SPEALTTANA LDIGDLVSFY RQAKQRFDAD EAFQETARQE VVRLQAGATD TLHAWKLLCE
QSRQEFQVIY DLLDVKLTER GESFYNPLLP TVVEGLEASG LLVENQGAKC VFLDGFTNRE
GEPLPLIVQK SDGGYNYATT DLAALRYRIQ KDEAKRIVYV TDAGQANHFA QFFQVARKAG
WIPNDVELVH VPFGLVLGED GKKFKTRSGD TVRLRDLLDE AVSRAHADLE ERLKAEEREE
TPEFIDKVAE VVGISAVKYA DLSQNRTSNY IFSYDKMLDL KGNTAPYMLY AYARIQGISR
KGGINFADLG DNAKVILQHD TEFALAKYLL QLGEVISTVE ADLLPNRLCE YLYELSKKFN
TFYDRNQGVQ VLSAEEPLRT SRLVLCDLTA RTLKLGLSLL GIQVLERM