EXO5_CANAL
ID EXO5_CANAL Reviewed; 628 AA.
AC Q59ZZ6; A0A1D8PSI4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 74.
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=DEM1; Synonyms=EXO5; OrderedLocusNames=CAALFM_CR03490WA;
GN ORFNames=CaO19.11870, CaO19.4392;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AOW31087.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP017630; AOW31087.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_715168.2; XM_710075.2.
DR AlphaFoldDB; Q59ZZ6; -.
DR STRING; 237561.Q59ZZ6; -.
DR PRIDE; Q59ZZ6; -.
DR GeneID; 3643200; -.
DR KEGG; cal:CAALFM_CR03490WA; -.
DR CGD; CAL0000179448; DEM1.
DR eggNOG; ENOG502QR0P; Eukaryota.
DR HOGENOM; CLU_019985_0_0_1; -.
DR InParanoid; Q59ZZ6; -.
DR OrthoDB; 1601909at2759; -.
DR PRO; PR:Q59ZZ6; -.
DR Proteomes; UP000000559; Chromosome R.
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 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..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..628
FT /note="Exonuclease V, mitochondrial"
FT /id="PRO_0000285321"
FT REGION 37..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 586
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 628 AA; 72427 MW; 49AA7D8685397AE1 CRC64;
MSRFWHFKKF YFTSCYSMQR MRGKIFKNEP LVPMNVTSEH EQVQSISKEE SRSLSSNDLN
LSADSELQLE SEPEIESEQL KNHEDVYEII RSMVLAADTT LPRLSNNSLT GIYNHWKLNP
NDDLPLYNPT KYTPYEFHSQ YNQDRSYIIT PRLSVTKLLV SSWCELRSFY QVYSGSVRLP
STKAMTQGTK LHSKLEAEVH PEIDTTEIEQ FLISNAMSLR ELQTTVPAEE ETVVIDLGEV
EQLAVDWAEM LIERLFSLIM GAEAREILLH GYLNLKNRSF VTNKDEIRES SSVLVSGIVD
YIKLQNVTNP SDGTLFDDIH GFVDSAFDQV DNVPLVDLSQ FLPEAKQILQ NYDFRLTFTD
VKTRSARQIP RQESVLEAAK FQTFYYRHFF HLLSRDSRFT YFSLIENAER RGHDVDKPLS
ILTTISLLRK HYHIFFKDFV KLANGEPIGF SPFDDSAKSI PYDFVSMFQS SDEFSLANPN
HNHFLEQISA IDGIEYDSIL SPLLKVWKTP PTLRYLAARA SQLFNVFNEN IGDITSVEYR
YNKTSELLSE KVYDYNFSEF QAEVESASKF WNGEREVIPT EDLSRCSYCE FQSKCMVAGG
KTTEAVEKKT IGPKIRQFLN ECESSSKG
