ID   EXO5_VANPO              Reviewed;         554 AA.
AC   A7TMJ6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=Kpol_513p10;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480423; EDO16494.1; -; Genomic_DNA.
DR   RefSeq; XP_001644352.1; XM_001644302.1.
DR   AlphaFoldDB; A7TMJ6; -.
DR   STRING; 436907.A7TMJ6; -.
DR   EnsemblFungi; EDO16494; EDO16494; Kpol_513p10.
DR   GeneID; 5544678; -.
DR   KEGG; vpo:Kpol_513p10; -.
DR   eggNOG; ENOG502QR0P; Eukaryota.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   InParanoid; A7TMJ6; -.
DR   OMA; LQVMYYR; -.
DR   OrthoDB; 1601909at2759; -.
DR   PhylomeDB; A7TMJ6; -.
DR   Proteomes; UP000000267; 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   InterPro; IPR019190; EXOV.
DR   PANTHER; PTHR14464; PTHR14464; 1.
DR   Pfam; PF09810; Exo5; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA-binding; Exonuclease; Hydrolase; Iron; Iron-sulfur; Magnesium;
KW   Metal-binding; Mitochondrion; Nuclease; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..554
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000406690"
FT   BINDING         138
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         522
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         525
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         531
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  64775 MW;  07AD11D315F5EFDD CRC64;
     MLRCRSSINI LQLHSRFHTH EIIISSKESE ARTRITDEER LVIKRFPIFK NDSSYILPSS
     NKLTKVKKEH IALKIHKIKK LFGEDPNNVG YLNYHLPKSY PVPFEINNRA YDNSDGNGEN
     EKVRNRLSVT KLLTKRWCEL REAYDIYSET PLFEHKQIIE GKLVHQKLEE DIHPVTEDLE
     SFVEDFEVPI PTDNFHNHVD DLFSCSMRLL SLFRCGEARE VRCHAFLDSR TGTFIDGLPK
     DGKDVLVSGI IDHLSLRRKI RVFTSSGFTE FNGLNDEVFE NGNNFQSIIE WLNANIDFLK
     SEYQINVSDV KTRMFRSVVS QKSVLKYSKY QVMYYRYFLE LLGLHPDVTY GQLLNSSLSR
     GFNIDQRIDP AKVIYFMASD EVIVDDMRKL RDGDDIGFPP FDSDFTGSSP TEEEYDMSIL
     SDQITDPNVL ERYGEFLVPW KRPVTLKYFA ARLAQMYNCI SPLLSKHLTL EYYYKGDNFK
     NINFDFNEDE IRNGAFDSSM FWFGKRDIEP IEPTSENLIT YCKYCDYVNV CSWRQKATQQ
     KKELGPRLLK LNQN