ID   EXO5_CANAW              Reviewed;         611 AA.
AC   C4YLG6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 45.
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=CAWG_01684;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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; CM000309; EEQ43447.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YLG6; -.
DR   STRING; 5476.C4YLG6; -.
DR   EnsemblFungi; EEQ43447; EEQ43447; CAWG_01684.
DR   VEuPathDB; FungiDB:CAWG_01684; -.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   OMA; LQVMYYR; -.
DR   Proteomes; UP000001429; Chromosome R.
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; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..611
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000406684"
FT   REGION          19..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         147
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         569
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         578
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   611 AA;  70269 MW;  7C32114E3A5BFE6C CRC64;
     MQRMRGKIFK NEPLVPMNVT SEHEQVQSIS KEESRSLSSN DLNLSADSEL QLESEPEIES
     EQLKNHEDVY EIIRSMVLAT DTTLPRLSNN SLTGIYNHWK LNPNDDLPLY NPTKYIPYEF
     HSQYNQDRSY IITPRLSVTK LLVSSWCELR SFYQVYSGSV RLPSTKAMTQ GTKLHSKLEA
     EIHPEIDTTE IEQFLISNAM SLRELQTTVP AEEETVVIDL GEVEQLAVDW AEMLIERLFS
     LIMGAEAREI LLHGYLNLKN RSFVTNKDEI RESSSVLVSG IVDYIKFQNV TNPSDGTLFD
     DIHGFVDSAF DQVDNVPLVD LSQFLPEAKQ ILQNYDFRLT FTDVKTRSAR QIPRQESVLE
     AAKFQTFYYR HFFHLLSRDS RFTYFSLIEN AERRGHDVDK PLSILTTISL LRKHYHIFFK
     DFVKLANGEP IGFSPFDDSA KSIPYDFVSM FQSSDEFSLA NPNHNHFLEQ ISAIDGIEYD
     SILSPLLKVW KTPPTLRYLA ARASQLFNVF NENIGDITSV EYRYNKTSEL LSEKVYDYNF
     SEFQAEVESA SKFWNGEREV IPTEDLSRCS YCEFQSKCMV AGGKTTEAVE KKTIGPKIRQ
     FLNECESSSK G