ID   EXO5_YEAS7              Reviewed;         585 AA.
AC   A6ZLA6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=SCY_0376;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000011; EDN64775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZLA6; -.
DR   EnsemblFungi; EDN64775; EDN64775; SCY_0376.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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_0000406694"
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;  67520 MW;  F5F7B5BD3A599FF9 CRC64;
     MLGRTLINKH GFLIHPRRFV HLNDKSLDGT FILPSKKNHM YDVPTNDPSG ILNASDIDRI
     NNLPFFDNTS PTKETNTKEG ALLSEKLASV KELFGEDPEN 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