SYR_PARMW
ID SYR_PARMW Reviewed; 597 AA.
AC Q7U3V8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SYNW2319;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(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; BX569695; CAE08834.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7U3V8; -.
DR SMR; Q7U3V8; -.
DR STRING; 84588.SYNW2319; -.
DR EnsemblBacteria; CAE08834; CAE08834; SYNW2319.
DR KEGG; syw:SYNW2319; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_3; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000001422; 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..597
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151626"
FT MOTIF 137..147
FT /note="'HIGH' region"
SQ SEQUENCE 597 AA; 65486 MW; EC115129CA50D277 CRC64;
MPDVPALMLS LSNTLDAQLR AAMQRAFPVA DAVLDPQLAP ASKPEFGDFQ ANGALPLAKP
LKQAPRQIAT AIVEQLQADS GFTDLCLEPQ IAGPGFINLT IRPERLAAEV SARLGDERLG
VPAVEQAAPV VVDFSSPNIA KEMHVGHLRS TIIGDSLARV LEFRGHTVLR LNHVGDWGTQ
FGMLITHLKQ VAPDALETAD AVDLGDLVAF YREAKKRFDD DEAFQSTSRE EVVKLQGGDP
VSLKAWGLLC DQSRREFQKI YDRLDIRLNE RGESFYNPFL PAVIDGLKAA ELLVTDDGAQ
CVFLEGVQGK DGKPLPVIVQ KSDGGFNYAT TDLAAIRYRF GAAPDGDGAR RVVYVTDAGQ
ANHFAGVFQV AERAGWIPDG ARLEHVPFGL VQGEDGKKLK TRAGDTVRLR DLLDEAVERA
ETDLRSRLKE EERSESEEFI QNVAGTVGLA AVKYADLSQN RITNYQFSFD RMLALQGNTA
PYLLYAVVRI AGIARKGGDL EVSTGQLQFS EPQEWALVRE LLKFDSVIAE VEEELLPNRL
CSYLFELSQV FNRFYDQVPV LKADPEALAS RLALCRLTAD TLRLGLGLLG IATLDRM