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 24-JAN-2024, entry version 141. 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; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, AND SUBCELLULAR 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., 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: This enzyme has both RNase and DNase activity. It degrades CC single-stranded DNA and RNA. {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 other CC interactions are via water molecules. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family. CC {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 AlphaFoldDB; Q10480; -. DR SMR; Q10480; -. DR BioGRID; 278759; 14. DR STRING; 284812.Q10480; -. DR iPTMnet; Q10480; -. DR MaxQB; Q10480; -. DR PaxDb; 4896-SPAC17C9-08-1; -. DR EnsemblFungi; SPAC17C9.08.1; SPAC17C9.08.1:pep; SPAC17C9.08. DR GeneID; 2542291; -. DR KEGG; spo:SPAC17C9.08; -. DR PomBase; SPAC17C9.08; pnu1. DR VEuPathDB; FungiDB:SPAC17C9.08; -. DR eggNOG; KOG3721; Eukaryota. DR HOGENOM; CLU_055174_0_2_1; -. DR InParanoid; Q10480; -. DR OMA; YVMPNQV; -. DR PhylomeDB; Q10480; -. DR PRO; PR:Q10480; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:PomBase. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005736; C:RNA polymerase I complex; IDA:PomBase. DR GO; GO:0004520; F:DNA endonuclease activity; IMP:PomBase. DR GO; GO:0004536; F:DNA nuclease activity; EXP:PomBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004521; F:RNA endonuclease activity; IDA:PomBase. DR GO; GO:0004540; F:RNA nuclease activity; EXP:PomBase. DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:PomBase. DR GO; GO:0032043; P:mitochondrial DNA catabolic process; EXP:PomBase. DR GO; GO:0000957; P:mitochondrial RNA catabolic process; EXP:PomBase. DR GO; GO:0006362; P:transcription elongation by RNA polymerase I; EXP:PomBase. DR CDD; cd00091; NUC; 1. DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1. DR InterPro; IPR018524; DNA/RNA_endonuclease_AS. DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease. DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf. DR InterPro; IPR020821; Extracellular_endonuc_su_A. DR InterPro; IPR044925; His-Me_finger_sf. DR InterPro; IPR040255; Non-specific_endonuclease. DR PANTHER; PTHR13966:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1. DR PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1. DR Pfam; PF01223; Endonuclease_NS; 1. DR SMART; SM00892; Endonuclease_NS; 1. DR SMART; SM00477; NUC; 1. DR SUPFAM; SSF54060; His-Me finger endonucleases; 1. DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1. PE 2: Evidence at transcript level; KW Endonuclease; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Nuclease; Reference proteome; KW Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT CHAIN ?..322 FT /note="Nuclease 1, mitochondrial" FT /id="PRO_0000019921" FT ACT_SITE 142 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10047" FT BINDING 174 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT CONFLICT 321..322 FT /note="GK -> VFLVFPVIVLYYENI (in Ref. 2; CAA97354)" FT /evidence="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 //