ID   NUC1_YEAST              Reviewed;         329 AA.
AC   P08466; D6VVY6;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Mitochondrial nuclease;
DE            EC=3.1.30.-;
GN   Name=NUC1; OrderedLocusNames=YJL208C; ORFNames=HRE329, J0310;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2935-106;
RX   PubMed=2836792; DOI=10.1093/nar/16.8.3297;
RA   Vincent R.D., Hofmann T.J., Zassenhaus H.P.;
RT   "Sequence and expression of NUC1, the gene encoding the mitochondrial
RT   nuclease in Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 16:3297-3312(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7754713; DOI=10.1002/yea.320100912;
RA   Purnelle B., Coster F., Goffeau A.;
RT   "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT   identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT   CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT   homologues to chromosome III genes.";
RL   Yeast 10:1235-1249(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7725802; DOI=10.1002/yea.320101216;
RA   Vandenbol M., Durand P., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT   "Sequence analysis of a 40.2 kb DNA fragment located near the left telomere
RT   of yeast chromosome X.";
RL   Yeast 10:1657-1662(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-329.
RX   PubMed=2552292; DOI=10.1128/mcb.9.8.3323-3331.1989;
RA   Liu Y., Dieckmann C.L.;
RT   "Overproduction of yeast viruslike particles by strains deficient in a
RT   mitochondrial nuclease.";
RL   Mol. Cell. Biol. 9:3323-3331(1989).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: This enzyme has both RNase and DNase activity.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; X06670; CAA29870.1; -; Genomic_DNA.
DR   EMBL; X77688; CAA54748.1; -; Genomic_DNA.
DR   EMBL; Z34098; CAA84003.1; -; Genomic_DNA.
DR   EMBL; Z49483; CAA89505.1; -; Genomic_DNA.
DR   EMBL; M28067; AAA34457.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08602.1; -; Genomic_DNA.
DR   PIR; S05888; NCBYN1.
DR   RefSeq; NP_012327.1; NM_001181641.1.
DR   AlphaFoldDB; P08466; -.
DR   SMR; P08466; -.
DR   BioGRID; 33550; 149.
DR   DIP; DIP-5041N; -.
DR   IntAct; P08466; 6.
DR   STRING; 4932.YJL208C; -.
DR   SwissPalm; P08466; -.
DR   MaxQB; P08466; -.
DR   PaxDb; 4932-YJL208C; -.
DR   PeptideAtlas; P08466; -.
DR   TopDownProteomics; P08466; -.
DR   EnsemblFungi; YJL208C_mRNA; YJL208C; YJL208C.
DR   GeneID; 853222; -.
DR   KEGG; sce:YJL208C; -.
DR   AGR; SGD:S000003744; -.
DR   SGD; S000003744; NUC1.
DR   VEuPathDB; FungiDB:YJL208C; -.
DR   eggNOG; KOG3721; Eukaryota.
DR   GeneTree; ENSGT00940000160987; -.
DR   HOGENOM; CLU_055174_0_2_1; -.
DR   InParanoid; P08466; -.
DR   OMA; YVMPNQV; -.
DR   OrthoDB; 5487361at2759; -.
DR   BioCyc; YEAST:G3O-31636-MONOMER; -.
DR   BioGRID-ORCS; 853222; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P08466; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P08466; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0004520; F:DNA endonuclease activity; IDA:SGD.
DR   GO; GO:0004529; F:DNA exonuclease activity; IDA:SGD.
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; IBA:GO_Central.
DR   GO; GO:0004540; F:RNA nuclease activity; IDA:SGD.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IMP:SGD.
DR   GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR   GO; GO:0051607; P:defense response to virus; IDA:SGD.
DR   GO; GO:0006308; P:DNA catabolic process; IDA:SGD.
DR   GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR   GO; GO:0006401; P:RNA catabolic process; IDA:SGD.
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   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Nuclease; Reference proteome.
FT   CHAIN           1..329
FT                   /note="Mitochondrial nuclease"
FT                   /id="PRO_0000178670"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10047"
FT   BINDING         170
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  37210 MW;  CAEC9678CB00943C CRC64;
     MCSRILLSGL VGLGAGTGLT YLLLNKHSPT QIIETPYPPT QKPNSNIQSH SFNVDPSGFF
     KYGFPGPIHD LQNREEFISC YNRQTQNPYW VLEHITPESL AARNADRKNS FFKEDEVIPE
     KFRGKLRDYF RSGYDRGHQA PAADAKFSQQ AMDDTFYLSN MCPQVGEGFN RDYWAHLEYF
     CRGLTKKYKS VRIVTGPLYL PKKDPIDNKF RVNYEVIGNP PSIAVPTHFF KLIVAEAPTA
     NPAREDIAVA AFVLPNEPIS NETKLTDFEV PIDALERSTG LELLQKVPPS KKKALCKEVN
     CQIVVRDFSN AAIKQSKDVK LLPPPKKRN
//