ID   EXO5_KOMPG              Reviewed;         543 AA.
AC   C4R7Q5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=PAS_chr4_0382;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(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; FN392322; CAY71630.1; -; Genomic_DNA.
DR   RefSeq; XP_002493809.1; XM_002493764.1.
DR   AlphaFoldDB; C4R7Q5; -.
DR   STRING; 644223.C4R7Q5; -.
DR   EnsemblFungi; CAY71630; CAY71630; PAS_chr4_0382.
DR   GeneID; 8200666; -.
DR   KEGG; ppa:PAS_chr4_0382; -.
DR   eggNOG; ENOG502QR0P; Eukaryota.
DR   HOGENOM; CLU_019985_0_0_1; -.
DR   InParanoid; C4R7Q5; -.
DR   OMA; LQVMYYR; -.
DR   Proteomes; UP000000314; Chromosome 4.
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..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..543
FT                   /note="Exonuclease V, mitochondrial"
FT                   /id="PRO_0000406689"
FT   BINDING         131
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         524
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         527
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         533
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   543 AA;  61980 MW;  E34D68E8F8064DF4 CRC64;
     MLEKGTQSLV NRTIKLRVLG GLTKKLAAPQ NESLPELKPQ LDVYQKFLEN LRAFPTKNKS
     VPNSPIRYSY YKIANKESEA VNRNLLELFA SKKYLPFLAS EIPKLPPPYV AAAAPMNPKI
     SVTQLLTDSW CELRSYYDSY ACSRAAPSAA MVSGTEQHKS LEDRTHKPEI NVTKEIQKNF
     TPIMMDQLKN FERTLNLISR FIDLLTIGKA REFAVTAIIN KETKELIDVN NLQKLAFVHQ
     KSPCYNDQFI LASGYLDYLR SESYVNGLEK EKWIQNNYSL NTLLETSIKG PLTVIDVKTR
     GKPIVTKSKG VLIGHRYQIG LYRKFLGLMS GENVSGINSP ISVDQINETA YTLLVTDSVQ
     RGYDVDEPVD PVVGLVMLAN NPWIITMLEQ ICVNDLLGNS LYDTFHAQQS TDYSWDLSQV
     NPKDFYQVLE PSLLQRTEQL FTKWKRPLSL RSITALISKF YPLISKKLSQ NTKIMYYTDG
     ECFHTSNYLY NPKAINTFME DKVKFLIGQR PPRPIEKSEI PQKCGFCRFQ SICEYSNLYN
     PVT