ID   EXO5_ZYGRC              Reviewed;         543 AA.
AC   C5DXZ1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
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; OrderedLocusNames=ZYRO0F08910g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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; CU928178; CAR28652.1; -; Genomic_DNA.
DR   RefSeq; XP_002497585.1; XM_002497540.1.
DR   AlphaFoldDB; C5DXZ1; -.
DR   STRING; 559307.C5DXZ1; -.
DR   EnsemblFungi; CAR28652; CAR28652; ZYRO0F08910g.
DR   GeneID; 8205348; -.
DR   KEGG; zro:ZYRO0F08910g; -.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   InParanoid; C5DXZ1; -.
DR   Proteomes; UP000008536; Chromosome F.
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..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..543
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000406696"
FT   BINDING         127
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         511
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         514
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   543 AA;  63105 MW;  BDA446DBA7F46D7B CRC64;
     MLRSRTKCAN SLLQIRKKSH LRQVISFSSR ELGLTEHELE TIDKLPFFDQ DRVNTRKRYP
     TTKRQAYLNE KLPAVKLLFG EDPQYPGFIS HSLPSMMPIP FEATQGTDEE TIANRLSVTK
     LLTKSWCELR HAYDVYAKIP MFEGKPIIKG KEEHQRLEDE THSLAEEQRA FEKDFEVVIP
     DDDFHKLAES WFASLVKMVN LFTDGEAREV LCHGYLNKKK ARLVEGPIIG DDDDDVLVSG
     IIDHLILKLR DVPVSNNVLP LRLENAIVSK NCEDIAVVFD QLERAGPNLQ NKFEIMVSDV
     KTRFMRKIPS QPSVLKASKL QVMYYRYFME VLGQNPQETY NKLLINAQRR GFDVNRFIDP
     AKVLSMMATD DMIRMDMYRL KNGDAIGFEP FDDSELNVSE SATYDMSDYH DIITDARVIQ
     KYSDFFEPWA KPVTLKYFAA RLAQMYHHLR PLLSNKLMIE YYYNGDNFHN IIFEFDPKLL
     RESSSDSAKF WFGQRDIEPI SRNLKNFLTF CKYCDYESVC SWKRGGNDMC KELGTDLAKI
     QKS