ID   EXO5_CANGA              Reviewed;         503 AA.
AC   Q6FJK6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=CAGL0M05577g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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.
CC   -!- SIMILARITY: Belongs to the EXO5 family. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62564.1; -; Genomic_DNA.
DR   RefSeq; XP_449588.1; XM_449588.1.
DR   AlphaFoldDB; Q6FJK6; -.
DR   STRING; 5478.XP_449588.1; -.
DR   EnsemblFungi; CAG62564; CAG62564; CAGL0M05577g.
DR   GeneID; 2891636; -.
DR   KEGG; cgr:CAGL0M05577g; -.
DR   CGD; CAL0137347; CAGL0M05577g.
DR   VEuPathDB; FungiDB:CAGL0M05577g; -.
DR   eggNOG; ENOG502QR0P; Eukaryota.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   InParanoid; Q6FJK6; -.
DR   OMA; LQVMYYR; -.
DR   Proteomes; UP000002428; Chromosome M.
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:EnsemblFungi.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
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; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..503
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000285322"
FT   BINDING         92
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         470
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   503 AA;  58260 MW;  67736AE7F9C37DDB CRC64;
     MTLRDVEKLR LWRLKIFRNQ QPILRAKPPH ASRKTQYLFQ KIDNVKSQFG TDGKGDLLWQ
     RDGMNPYHDL YDPGDLKTHR LSVTKLLTKS WCELRFAYDL YSRLPLFREA HLAAGERTHQ
     KLENSEHTPV IRPQDIPQFS ETVEIVEDDL HVLAASWAET ITRLIHLFSS GDAREILCHG
     YLNKETNQLY DPMETEVWDP SQHILISGII DHLTLTSKNG NLPLNNHHRS IDDSIAKLKN
     TRNEFAKNGL TIQISDVKTR TRKFIPPQES VQNATKLQLM YYRHFLLSLG TDSDNTYEML
     LYNARIRGVD VDQPLNPANC LLIMIQMDGF VGDFVKLQNG DGFQFPKFDN APISHSFTLA
     DAKHHQFLQN INSHELAGQL LNGTFAKPIT LRYFAMRLAQ MYSMLTPLIS EKLKVEYYHN
     NECFQEVEFV NDKKSLGESC RSASSFWFGK RAIEPVEATT FNYNQYCKHC DYRDHCAWIK
     DSLAKSTKLG DELTQIARRI HNI