ID   YDH5_SCHPO              Reviewed;         285 AA.
AC   Q92350;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable nudix hydrolase C6G9.05;
DE            EC=3.6.1.-;
GN   ORFNames=SPAC6G9.05;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC       diphosphate derivatives. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB03607.1; -; Genomic_DNA.
DR   PIR; T39067; T39067.
DR   RefSeq; NP_594114.1; NM_001019538.2.
DR   AlphaFoldDB; Q92350; -.
DR   SMR; Q92350; -.
DR   BioGRID; 278011; 2.
DR   STRING; 4896.SPAC6G9.05.1; -.
DR   MaxQB; Q92350; -.
DR   PaxDb; Q92350; -.
DR   EnsemblFungi; SPAC6G9.05.1; SPAC6G9.05.1:pep; SPAC6G9.05.
DR   PomBase; SPAC6G9.05; -.
DR   VEuPathDB; FungiDB:SPAC6G9.05; -.
DR   eggNOG; KOG3069; Eukaryota.
DR   HOGENOM; CLU_977146_0_0_1; -.
DR   InParanoid; Q92350; -.
DR   OMA; HAGQMCF; -.
DR   PhylomeDB; Q92350; -.
DR   PRO; PR:Q92350; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005777; C:peroxisome; ISO:PomBase.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0010945; F:CoA pyrophosphatase activity; ISS:PomBase.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:1990748; P:cellular detoxification; TAS:PomBase.
DR   GO; GO:0015938; P:coenzyme A catabolic process; IBA:GO_Central.
DR   GO; GO:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro.
DR   CDD; cd03426; CoAse; 1.
DR   InterPro; IPR045121; CoAse.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR000059; NUDIX_hydrolase_NudL_CS.
DR   PANTHER; PTHR12992; PTHR12992; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS01293; NUDIX_COA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..285
FT                   /note="Probable nudix hydrolase C6G9.05"
FT                   /id="PRO_0000057143"
FT   DOMAIN          114..254
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           153..175
FT                   /note="Nudix box"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   285 AA;  32772 MW;  CDB0B46B5545154E CRC64;
     MKLKLRWKGH QRFLTRQNSL VGFIWSPLKN TFSKRNSILN NQVCFEAIKY IQRHYFSSQS
     HHVTYLHQSP LEKLVSNGVV NENGDLTMDS LSHQIYLLHK NRPTLPLKPT NQPTRFASVL
     MPLVNTSQGA SLLLTQRSPN LRSHAGQMCF PGGRVEPSDG SHYYAALRET YEEIGFLPNF
     FTYLTTFPPL FTRDEKTEIR AYLAFSVQTS LPSLGTGEVK DLFYVPLTSF LNPKHQKISR
     FRNTDLLYVE FNIDKIPRIW GITAVILNMY LNSICPDALI SIPKF