SYR_PROMA
ID SYR_PROMA Reviewed; 603 AA.
AC Q7VE03;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Pro_0212;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAP99258.1; -; Genomic_DNA.
DR RefSeq; NP_874606.1; NC_005042.1.
DR RefSeq; WP_011124367.1; NC_005042.1.
DR AlphaFoldDB; Q7VE03; -.
DR SMR; Q7VE03; -.
DR STRING; 167539.Pro_0212; -.
DR PRIDE; Q7VE03; -.
DR EnsemblBacteria; AAP99258; AAP99258; Pro_0212.
DR GeneID; 54199571; -.
DR KEGG; pma:Pro_0212; -.
DR PATRIC; fig|167539.5.peg.219; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_3; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001420; 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; Reference proteome.
FT CHAIN 1..603
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151589"
FT MOTIF 143..153
FT /note="'HIGH' region"
SQ SEQUENCE 603 AA; 67957 MW; 47480307399C3839 CRC64;
MYNIYKSLNQ QVQRALNTAF PEAASQVKES GDFLNPQLVA ATKPEFGDFQ INGALALARI
IKKSPRQIAE ILIKQLESNE VFKAICLPPE IAGPGFINLT LQNTCLINEI TSRLNDDLLG
VPLVNDDEIT KKLKPVIVDF SSPNIAKEMH VGHLRSTIIG DSIARILNYR GYKVIRLNHV
GDWGTQFGML ITHLKEVAPK ALTTANVINL GNLVEFYKKA KQRFDEDEYF QQCSRNEVVN
LQRGNKESLK AWELLCEQSR KEFNKIYDRL KIEISERGES FYNPFLQGVI DDLTRSGLLV
EDDGAKCVFL NGINGKDGNP LPLIIQKADG GFNYATTDLA AIRYRLKDQP DGDGAGRIIY
VTDSGQANHF AGVFQVAKRA KWLPSSSRIE HVPFGLVQGE DGKKLKTRSG ETVRLKDLLD
EAISRAKLDI ERRLNEENRK ESQAFIEKVS NTIGIAAVKY ADLSQNRITN YQFSFDRMLA
LQGNTAPYLL YAVVRIAGIN RKGGDLHSSV NKLNFSEPQE WRLIRELLKF DEVIIAVEEE
LLPNRLCNYL FELSQVFNRF YDQIPVLKAE EPSRSCRLAL CQLTGDTLKK GLNLLGISTL
ERM