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Database: UniProt
Entry: Q9A0Y2_STRP1
LinkDB: Q9A0Y2_STRP1
Original site: Q9A0Y2_STRP1 
ID   Q9A0Y2_STRP1            Unreviewed;       274 AA.
AC   Q9A0Y2; Q48ZY8;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
GN   OrderedLocusNames=SPy_0559 {ECO:0000313|EMBL:AAK33549.1};
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447 {ECO:0000313|EMBL:AAK33549.1, ECO:0000313|Proteomes:UP000000750};
RN   [1] {ECO:0000313|EMBL:AAK33549.1, ECO:0000313|Proteomes:UP000000750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1
RC   {ECO:0000313|Proteomes:UP000000750};
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Adjic D., Savic D., Savic G., Lyon K.,
RA   Primeaux C., Sezate S.S., Surorov A.N., Kenton S., Lai H., Lin S., Qian Y.,
RA   Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
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DR   EMBL; AE004092; AAK33549.1; -; Genomic_DNA.
DR   RefSeq; NP_268828.1; NC_002737.2.
DR   AlphaFoldDB; Q9A0Y2; -.
DR   KEGG; spy:SPy_0559; -.
DR   PATRIC; fig|160490.10.peg.479; -.
DR   HOGENOM; CLU_004553_2_6_9; -.
DR   OMA; CHVECEL; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000750}.
FT   DOMAIN          46..274
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   274 AA;  31994 MW;  138397AAC56099C9 CRC64;
     MGLGSDSLPV KISLFDVDTY LADSMQFHLE YILRLFPKSG VHYLMPTFRG EAVDHRHLSQ
     FYHSECEIEG DLHYVMNLVD RYIKFLVSEI LRECRDSIFA ITKDVSHLES FIDRKIPIIT
     FEEACTILEN EIDSLEYNDE HHFYVLTDVG EKKLMEHFEG VVWVKNYPCK SVPFYQRFST
     DHLFAYNADL LLGIGETVGC GERCETYEEV VENMNYLQVD ASEYSWYLEM KKTRPMKSSG
     FGLGVERLIA WILKCDDVRK VQLISRENGI DYLP
//
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