EXO5_CANDC
ID EXO5_CANDC Reviewed; 624 AA.
AC B9WLF5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=CD36_28710;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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; FM992695; CAX39916.1; -; Genomic_DNA.
DR RefSeq; XP_002421916.1; XM_002421871.1.
DR AlphaFoldDB; B9WLF5; -.
DR STRING; 42374.XP_002421916.1; -.
DR EnsemblFungi; CAX39916; CAX39916; CD36_28710.
DR GeneID; 8050229; -.
DR KEGG; cdu:CD36_28710; -.
DR CGD; CAL0000171417; Cd36_28710.
DR VEuPathDB; FungiDB:CD36_28710; -.
DR eggNOG; ENOG502QR0P; Eukaryota.
DR HOGENOM; CLU_019985_0_0_1; -.
DR OrthoDB; 1601909at2759; -.
DR Proteomes; UP000002605; Chromosome R.
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; Transit peptide.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 62..624
FT /note="Exonuclease V, mitochondrial"
FT /id="PRO_0000406685"
FT REGION 37..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 582
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 591
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 624 AA; 72071 MW; 66C6A9F2A6CC7D5A CRC64;
MSRFWHFKKF YFSSCFSKQR MSRRIIKNEL LVPMKVTSKH EQEQPITNDE PRSLLSEDAN
PSPDVESEPE LESEQSENRE DVHEIIRSMV LGTGTTLPRL SNDSLTGIYN YWKLNPNDDL
PLYNPTKYTP FEFHSQYNQD RSYISTPRLS VTKLLVFSWC ELRSFYQVYS GSVRLPSTQA
MTQGTKLHSK LEAEIHPEID TTEIEQFLLS NAMSLGELQK AVPIEEDKVV FYLGEVERLA
VDWAEMLIER LFSLIMGAEA REILLHGYLN FNNRSFVTNK DEIRDPSSVL VSGIVDYVKL
QNLTNPSDGT LFDDIHGFVD DNFDQVDNVP LVDLSKFLPE AKQILQHYDF RLTFTDVKTR
SAPQIPRQES VLEAAKFQTF YYRHFFQLLS RDSRFTYFSL IENAERRGHD VDKPLSILTT
ICLLRKHYHI LFKDFVRLAN GEPIGFAPFD DSAKSMAYDF VSVFQSSDEF SLANPNHTHF
FEQLREIDGI EYDSILSPLL KVWKTPPTLR YLAARASQLF GVFEENLGDV TSVEYRLNKT
SQLLSENVYE YDFSEFQVEV ESASKFWNGE REAVPTEDLS RCSFCEFQSK CMVAGGNTTE
AVEKKTIGPK IRHFLNECES SSKG