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 27-MAR-2024, entry version 125.
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; 284812.Q92350; -.
DR MaxQB; Q92350; -.
DR PaxDb; 4896-SPAC6G9-05-1; -.
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; SHAGQMC; -.
DR PhylomeDB; Q92350; -.
DR Reactome; R-SPO-9033241; Peroxisomal protein import.
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:0010945; F:coenzyme A diphosphatase 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 Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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; NUDIX HYDROLASE; 1.
DR PANTHER; PTHR12992:SF24; PEROXISOMAL COENZYME A DIPHOSPHATASE NUDT7; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 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
//
