ID PNU1_SCHPO Reviewed; 322 AA. AC Q10480; Q9HFA0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 08-JUN-2016, entry version 107. DE RecName: Full=Nuclease 1, mitochondrial; DE EC=3.1.30.-; DE AltName: Full=SpNUC1; DE Flags: Precursor; GN Name=pnu1; Synonyms=nuc1; ORFNames=SPAC17C9.08; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, AND SUBCELLULAR RP LOCATION. RC STRAIN=ATCC 87289; RX PubMed=11406279; DOI=10.1016/S0167-4781(01)00206-8; RA Ikeda S., Kawasaki N.; RT "Isolation and characterization of the Schizosaccharomyces pombe cDNA RT encoding the mitochondrial endonuclease."; RL Biochim. Biophys. Acta 1519:111-116(2001). RN [2] 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: This enzyme has both RNase and DNase activity. It CC degrades single-stranded DNA and RNA. CC {ECO:0000269|PubMed:11406279}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:11406279}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:11406279}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:11406279}. CC -!- MISCELLANEOUS: The active site contains 1 hydrated divalent metal CC cation that has only 1 direct interaction with the protein; all CC other interactions are via water molecules. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB050780; BAB20882.1; -; mRNA. DR EMBL; CU329670; CAA97354.2; -; Genomic_DNA. DR PIR; T11588; T11588. DR RefSeq; NP_594598.2; NM_001020026.3. DR ProteinModelPortal; Q10480; -. DR BioGrid; 278759; 14. DR MaxQB; Q10480; -. DR EnsemblFungi; SPAC17C9.08.1; SPAC17C9.08.1:pep; SPAC17C9.08. DR GeneID; 2542291; -. DR KEGG; spo:SPAC17C9.08; -. DR EuPathDB; FungiDB:SPAC17C9.08; -. DR PomBase; SPAC17C9.08; pnu1. DR HOGENOM; HOG000214172; -. DR InParanoid; Q10480; -. DR KO; K01173; -. DR OMA; ETITQES; -. DR OrthoDB; EOG7034SQ; -. DR PhylomeDB; Q10480; -. DR PRO; PR:Q10480; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:PomBase. DR GO; GO:0004520; F:endodeoxyribonuclease activity; IMP:PomBase. DR GO; GO:0004521; F:endoribonuclease activity; IDA:PomBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IMP:PomBase. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:PomBase. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:PomBase. DR GO; GO:0006308; P:DNA catabolic process; ISS:PomBase. DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IMP:PomBase. DR GO; GO:0006310; P:DNA recombination; ISS:PomBase. DR GO; GO:0006401; P:RNA catabolic process; IMP:PomBase. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:GOC. DR Gene3D; 3.40.570.10; -; 1. DR InterPro; IPR018524; DNA/RNA_endonuclease_AS. DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease. DR InterPro; IPR020821; Extracellular_endonuc_su_A. DR Pfam; PF01223; Endonuclease_NS; 1. DR SMART; SM00892; Endonuclease_NS; 1. DR SMART; SM00477; NUC; 1. DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endonuclease; Hydrolase; Magnesium; Manganese; KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Nuclease; Reference proteome; Transit peptide. FT TRANSIT 1 ? Mitochondrion. FT CHAIN ? 322 Nuclease 1, mitochondrial. FT /FTId=PRO_0000019921. FT ACT_SITE 142 142 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10047}. FT METAL 174 174 Magnesium or manganese; catalytic. FT {ECO:0000250}. FT CONFLICT 321 322 GK -> VFLVFPVIVLYYENI (in Ref. 2; FT CAA97354). {ECO:0000305}. SQ SEQUENCE 322 AA; 36428 MW; C3AB9C38801563A5 CRC64; MSSNLIKSFG LIAIGAISGV TFTHFYYKGY QGSDVPDLTP RYTKFDSAGR ALESIYDFNA TKFFQYGIPG PVADQRVNHG YMSVFDRRTR NPFYTAETIT QESLNQRKGN RRYSEFVPDD NIPEMFQAKL GDYRGSGYDR GHQVPAADCK FSQEAMNETF YLSNMCPQVG DGFNRNYWAY FEDWCRRLTS KYGSVTIMTG PLYLPKKNER GQWEVQYRVI GNPPNVAVPT HFFKVIIAEK SGEPTSSPSV AAFVLPNKPI ADNFPLKNFA VPVEVVERAS GLEILSNVPK GNRKQLCSEV VCQLNVKEFV ESVKQKQKNQ GK //