ID   EXO5_YEAS8              Reviewed;         585 AA.
AC   D3UEQ8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Exonuclease V, mitochondrial;
DE            Short=Exo V;
DE            EC=3.1.-.-;
DE   AltName: Full=Defects in morphology protein 1;
DE   Flags: Precursor;
GN   Name=EXO5; Synonyms=DEM1; ORFNames=EC1118_1B15_3235g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Single strand DNA specific 5' exonuclease involved in
CC       mitochondrial DNA replication and recombination. Releases dinucleotides
CC       as main products of catalysis. Has the capacity to slide across
CC       5'double-stranded DNA or 5'RNA sequences and resumes cutting two
CC       nucleotides downstream of the double-stranded-to-single-stranded
CC       junction or RNA-to-DNA junction, respectively (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EXO5 family. {ECO:0000305}.
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DR   EMBL; FN393060; CBK39238.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3UEQ8; -.
DR   EnsemblFungi; CBK39238; CBK39238; EC1118_1B15_3235g.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome II, Scaffold EC1118_1B15.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:InterPro.
DR   InterPro; IPR016610; Exo5.
DR   InterPro; IPR019190; EXOV.
DR   PANTHER; PTHR14464; PTHR14464; 1.
DR   Pfam; PF09810; Exo5; 1.
DR   PIRSF; PIRSF013220; UCP013220; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA-binding; Exonuclease; Hydrolase; Iron; Iron-sulfur; Magnesium;
KW   Metal-binding; Mitochondrion; Nuclease; Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..585
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000406695"
FT   BINDING         141
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         549
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         552
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         558
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   585 AA;  67552 MW;  485E77B4DF1F5E52 CRC64;
     MLGRTLINKH GFLIHPRRFV HLNDKSLDGT FILPSKKNHM YDVPTNDLSG ILNASDIDRI
     NNLPFFDNTS PTKETNTKEG ALLSEKLASV KELFGEDLEN PSFINYRFPR GLENPYFDIQ
     VNQLKKKRLS VTQLCTTQNW CELRNFYDFY SQNLSNQLLN LKFQVQKGKK IHKSLEDETH
     PELNQYKSFT HNFLALTKLS MDIDNDMDAL LDNWFNSINR LVSLFTKGDG HAREIVCHGF
     INLEDGKLVE HLLNSDSKTK ENVIISGVID HLTLRNKHNH QVQKGAAHLD TEYQSWGNIL
     TNLLSNLKEL KSNNEIVISD IKTRSVPKIP SIESVIESSK LQTMYYKFFF SHLSQDMTQT
     YHSFLINAKR RGLDVDAPIN PTKILTFILT NPLFANDVKN LLYGLPINHS AFDNDAKGSN
     TFDMAAFNDL LDRGPTSFNV PIEQDEDSSE STKCVSLRDY GHFYTKWKTP LTLKYFAARL
     SQIYFIVGNL VSNDLMIEYY YHNDNFHNII FPYDTLKLGT HAHDSAMVWF GGRDMHPIEP
     TQKNFNTYCK FCDYRHVCSW KNKNELKLID LGKELKKIIL ESSMK