ID   EXO5_LACTC              Reviewed;         552 AA.
AC   C5DIF1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=KLTH0E12012g;
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
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; CU928169; CAR23562.1; -; Genomic_DNA.
DR   RefSeq; XP_002553999.1; XM_002553953.1.
DR   AlphaFoldDB; C5DIF1; -.
DR   STRING; 559295.C5DIF1; -.
DR   EnsemblFungi; CAR23562; CAR23562; KLTH0E12012g.
DR   GeneID; 8292166; -.
DR   KEGG; lth:KLTH0E12012g; -.
DR   eggNOG; ENOG502QR0P; Eukaryota.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   InParanoid; C5DIF1; -.
DR   OMA; LQVMYYR; -.
DR   OrthoDB; 1601909at2759; -.
DR   Proteomes; UP000002036; Chromosome E.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..552
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000406688"
FT   BINDING         132
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   552 AA;  63638 MW;  A9D5A4B4B376ACD8 CRC64;
     MTLKRFSLFA RNIHLPKKTN AASVESNGSL APTDEELEVI NSLPPFQHAL QLSSQSATKA
     KRSYLETKLP KVQKLFKSSR DPAYLAYDFP QGLSNPYVDA HARPVTNPVT GDTKYRGTPR
     LSVTKLLTKR WCELRETYDI YSRIPIFEHS QVKQGRKEHQ RLEEEVHAPP ANIEEFEANF
     EVDIPDDPFH SLVEDWYLSI VRLVTLFQKG QAREILCHGY LSSRTSGFVR GKVKDDNDVL
     VSGIIDHLIL RQRRAKNNVP SSLTQVLSES VDINLAQFLN LLPSLVQQAS KDFEIVVSDV
     KTRSTKTIPR QQTVVKASKM QVMYYRFLLE DLGRDAETTY QKLLINAQRR GFNVDQPINP
     AKIINLLEID PMIRGDMERL QRGDQLGFKP FDSEAELNTS QPVYTLEEFD EKITDLRTRQ
     KYETLFTTWN TPVTLRYFAA RLALMYENVG PLLSQNLMIE YYCGDVNFHN ISFSFDAEEL
     ERQSFDSAQF WFGKRAIEPI KPNMKNLQTY CKYCDYESVC LWRKEGRQAC KTLGQELVRL
     YNGNSPNAIT RE