Y1686_STRCO
ID Y1686_STRCO Reviewed; 181 AA.
AC Q9S266;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Uncharacterized Nudix hydrolase SCO1686;
DE EC=3.6.-.-;
GN OrderedLocusNames=SCO1686; ORFNames=SCI30A.07;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AL939109; CAB46784.1; -; Genomic_DNA.
DR PIR; T36787; T36787.
DR RefSeq; NP_625960.1; NC_003888.3.
DR RefSeq; WP_011027918.1; NC_003888.3.
DR AlphaFoldDB; Q9S266; -.
DR SMR; Q9S266; -.
DR STRING; 100226.SCO1686; -.
DR GeneID; 1097117; -.
DR KEGG; sco:SCO1686; -.
DR PATRIC; fig|100226.15.peg.1703; -.
DR eggNOG; COG1443; Bacteria.
DR HOGENOM; CLU_060552_3_1_11; -.
DR InParanoid; Q9S266; -.
DR OMA; PGYWDVA; -.
DR PhylomeDB; Q9S266; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR024195; NUDIX_hydrolase_YfcD_pred.
DR Pfam; PF00293; NUDIX; 1.
DR PIRSF; PIRSF017340; Nudix_hydro; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..181
FT /note="Uncharacterized Nudix hydrolase SCO1686"
FT /id="PRO_0000057087"
FT DOMAIN 35..175
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 72..94
FT /note="Nudix box"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 181 AA; 19950 MW; 766642DC3C6F8428 CRC64;
MDGLMSSADE ILDIVDENDR VVGQARRGDA YARGLRHRCV FVWARDPEGR VFVHRRTATK
LVFPAPYDMF VGGVVGAGES YDDAALREAE EELGASGLPR PEFLFKFLYD DGAGRTWWSA
VYEVRVAGAV SPQVEEVAWH GFLPEAELEG RLGEWEFVPD GLSAYARLRA WRGASGPGSV
G