PNU1_SCHPO
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 03-AUG-2022, entry version 135.
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}.
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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; 4896.SPAC17C9.08.1; -.
DR MaxQB; Q10480; -.
DR PaxDb; Q10480; -.
DR PRIDE; Q10480; -.
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:0004520; F:endodeoxyribonuclease activity; IMP:PomBase.
DR GO; GO:0004519; F:endonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IDA: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: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 Gene3D; 3.40.570.10; -; 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; PTHR13966; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; SSF54060; 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
