ID   EXO5_CLAL4              Reviewed;         499 AA.
AC   C4Y732;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 44.
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=CLUG_03966;
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720;
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; CH408079; EEQ39838.1; -; Genomic_DNA.
DR   RefSeq; XP_002616725.1; XM_002616679.1.
DR   AlphaFoldDB; C4Y732; -.
DR   STRING; 306902.C4Y732; -.
DR   EnsemblFungi; EEQ39838; EEQ39838; CLUG_03966.
DR   GeneID; 8497084; -.
DR   KEGG; clu:CLUG_03966; -.
DR   VEuPathDB; FungiDB:CLUG_03966; -.
DR   HOGENOM; CLU_546279_0_0_1; -.
DR   InParanoid; C4Y732; -.
DR   OMA; LQVMYYR; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
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..12
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           13..499
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000406687"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  56099 MW;  A8109E913DABF4A9 CRC64;
     MSRVLTFRVP PEQQQAPKPL LSDRSSTWPL LPQLAPTAVR PASPPSPKEE LVLNVFGRGP
     DSLLMPPKHS LPPPFAFYTQ FNGDASYMAE PRLSVTKLLV SSWCELREYY EVYAGSPRRV
     PTARLTQGTD YHRVLEERSH RAIDPSTVSA RVEEILGEMP EERVLALTQG GSMAFKLAHQ
     WVEQILVRCL AVAHTGYARE MHLHGFLDLT SGELATSKST IGQGVLVNGI ADMVRLEPAP
     YGHDRALPWD PQAVLELGPA LEGAKARMDR LATNHTLEVR DVKTRAYNNV PKQSSVVEAA
     RDQCMYYAQF LTTLAQNEEY AYQSLVENFT RRHIQTSHPL GEAHAAALLI TNFGVLVEDY
     KALARGDALS FTPFDNATTF YVTEQPPEAY SLANFVDEPT FRTLLADFHG DYFADVDISV
     LFREWKRPLT PAYFCARAAQ ALYLFEKLKP SSVCVEYHNV KTGRIIECKS FPFDKHTLEE
     ASKRAAQFLG RYSTTHKHR