ID   EXO5_ASHGO              Reviewed;         527 AA.
AC   Q75A64;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=ADR054C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51974.1; -; Genomic_DNA.
DR   RefSeq; NP_984150.1; NM_209503.1.
DR   AlphaFoldDB; Q75A64; -.
DR   STRING; 33169.AAS51974; -.
DR   EnsemblFungi; AAS51974; AAS51974; AGOS_ADR054C.
DR   GeneID; 4620299; -.
DR   KEGG; ago:AGOS_ADR054C; -.
DR   eggNOG; ENOG502QR0P; Eukaryota.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   InParanoid; Q75A64; -.
DR   OMA; LQVMYYR; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
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; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..527
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000285320"
FT   BINDING         119
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         500
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         506
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   527 AA;  59075 MW;  79215A57EAED8784 CRC64;
     MRTVRQRWAT GWGRALHTSG SAPAGSSAES ALLPEMGQLD PKVAAAPRRK YLSAKYRVVG
     KLFQQAENGG YLAYRKPAAL ENPYLDVQAR PRVDGATGQI VYQGTPRLSV TRLLTKQWCE
     LRTAYDLYSN MPLFESKAMR IGKRAHRKLE NKLHGASDAA ATQALERLQL AVPVDPLHRL
     AADWAGAIDR MCTLFQKGEA RELLCHGYIS ADHGAFVEGP VREDSDVLVS GVIDHLVLTQ
     RGGGSPLSAL QPERSLQFPS DMAELVPFLK DLGERRAAEW EVVVGDIKTR KYTQVPSQAS
     VVETSRLQVM YYRRFLEDLG ADVDKAYEKL LTNAQRRGLD VDAPLAAGSA ISVMEGIPQL
     GADMLRLVRG DPIGFGPFDS YNRYAAHDTY DFTQHAALLQ DQPELQKYAV FFGQWKTPFN
     LRFLAARMAQ LYGCIAPLLS NTLLIEYYMG GECFHVNTFK YDAAELRKHC EDSARFWFGK
     REIEPIEPTI RNVNAYCKFC DYKDICLWRK EAVLGWKSLG EELRGLP