SYR_MAGMM
ID SYR_MAGMM Reviewed; 575 AA.
AC A0L5I2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Mmc1_0704;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK43225.1; -; Genomic_DNA.
DR RefSeq; WP_011712385.1; NC_008576.1.
DR AlphaFoldDB; A0L5I2; -.
DR SMR; A0L5I2; -.
DR STRING; 156889.Mmc1_0704; -.
DR PRIDE; A0L5I2; -.
DR EnsemblBacteria; ABK43225; ABK43225; Mmc1_0704.
DR KEGG; mgm:Mmc1_0704; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000002586; 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..575
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000095379"
FT MOTIF 130..140
FT /note="'HIGH' region"
SQ SEQUENCE 575 AA; 63647 MW; EDB8C99DE49200EB CRC64;
MRQSIEELME HAQNTLLAEG VIPADAKLGG IKVERPKDKS HGDFSINTAM VLAKQARMKP
RDLAQRLVDA LPSGQGVVSR CEIAGPGFIN FFVTPERLRG VVADVLQRGG SYGQGNVGAG
QKVLVEFVSA NPTGPMHVGH GRGAVTGDVL ARILECAGYA VQREYYLNDA GVQVQVLGRS
VMLRYRQLFG DAVEVAEGCY PGDYVVDIAR ALKEKDQDKW LEVARAEPDE YPREMLEFAM
QQVLTWIKAD LARLNIRFDH WFSEFSLHSE GRIEHALEVL SQKGCLYEGV LEPPKGKKSE
AWASRPQLLF KATDFGDEVD RALRKSDGSY TYFAADVAYH LNKAERGFER LVNIWGADHG
GYVRRVQAAL GALTGKQNLL DVVLIQMVNL TRGGEPVKMS KRAGTFVTLE EVVEATSSDA
VRFWFLSRGS GAQLDFDLDL AVAKNNDNPV YYVQYAHARI CSIWDKAQHE GVALQAQGWS
GVDLSPLGEG AEWDLIRKLD LFPDVVEGAA VHQEPHRIPY YLLDLAAAFH TFYNSHRIMD
VDAGTRDARL VLILAVKQVI ANGLELLGVQ QPRSM