SYR_MALP2
ID SYR_MALP2 Reviewed; 564 AA.
AC Q8EVF2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=MYPE6120;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC44402.1; -; Genomic_DNA.
DR RefSeq; WP_011077434.1; NC_004432.1.
DR AlphaFoldDB; Q8EVF2; -.
DR SMR; Q8EVF2; -.
DR STRING; 272633.26454072; -.
DR EnsemblBacteria; BAC44402; BAC44402; BAC44402.
DR KEGG; mpe:MYPE6120; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_14; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000002522; 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..564
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242052"
FT MOTIF 130..140
FT /note="'HIGH' region"
SQ SEQUENCE 564 AA; 65016 MW; 879573694136E010 CRC64;
MIKTTIIASI KDLIKDAVKD KFKITIDLND FVVDKAKSIE FGDFYSNVAM ILASKLKKNP
ILIAEEICEY LKNHKTNLFE STEAVKPGYI NVFLSNSVKS DLFKQINKDK DTYGIFEPKK
VAYNIEFVSA NPTGSLHIGH ARNAALGQTL GNVWKAYGYT IEQEYYINDG GNQINNLGMS
VFYRYLQKCG KDVQMEEDFY QGSEPIAVAE LIYKEHKDKF VNVKYSATKI EDEKVFDFFR
DFSKTELMNI IKKDLKDFSV HFDRYFPESK IYEMKLVDPT IKKLGKYVYE KDGALWLKTT
EFGDDKDRVI VKSDKSFTYF MPDIAYHDIK ATRTINGLKT DKIFNIWGAD HASYVDRMTV
ALQCLGFKKD IMHVIVMQMV KLTKNGKEFK MSKRSGNSLT LRDLINAIGV DNSRWELISQ
AAESHIEIDV EKFTSADSTS NLSYVLYAYS RIQKILEKNE SLLKESKSYN TDLLTNLKEK
DMIAMLFYYP QTIANIAKSY EVHKIPIFLY TLANLLHSYY SEVKIIDESN KELLIQRLHL
LQCVNQVIKN GLKLLDIEAK VLNK