EXO5_DEBHA
ID EXO5_DEBHA Reviewed; 630 AA.
AC Q6BKP5; B5RUJ8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
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=DEHA2F20240g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382138; CAR66376.1; -; Genomic_DNA.
DR RefSeq; XP_002770856.1; XM_002770810.1.
DR AlphaFoldDB; Q6BKP5; -.
DR STRING; 4959.XP_002770856.1; -.
DR EnsemblFungi; CAR66376; CAR66376; DEHA2F20240g.
DR GeneID; 8999018; -.
DR KEGG; dha:DEHA2F20240g; -.
DR VEuPathDB; FungiDB:DEHA2F20240g; -.
DR eggNOG; ENOG502QR0P; Eukaryota.
DR HOGENOM; CLU_019985_0_0_1; -.
DR InParanoid; Q6BKP5; -.
DR OMA; LQVMYYR; -.
DR OrthoDB; 1601909at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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 GO; GO:0000002; P:mitochondrial genome maintenance; IEA:InterPro.
DR InterPro; IPR016610; Exo5.
DR InterPro; IPR019190; EXOV.
DR PANTHER; PTHR14464; PTHR14464; 2.
DR Pfam; PF09810; Exo5; 2.
DR PIRSF; PIRSF013220; UCP013220; 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..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..630
FT /note="Exonuclease V, mitochondrial"
FT /id="PRO_0000285323"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 600
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 606
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 630 AA; 72633 MW; 11655DBF4393BB60 CRC64;
MIRPGKVLVL NFLKRSLSNL ATFKGSEINT KKYDLKLPNN SDSNKQYFTL DEKLKVIQYT
DANEESIIDE FILPLSSGAK ASDTYQKTNL SKMRNLLTTF HIDEGESLPL SKPGYIKETP
FEYHSKYNSD TSYVSIPRLS VTKLLTFQWC ELREFYTIFS GSPVKKETKE MKLGTEAHLK
LELETHNLID VEDIERITDE FVEKKIDSSK RHINTLADPD DILLAKDDLS KLTELLHGAI
PESSMANEWM SKIISRLFTL INTSEAREVL VHGYLDFQTS HFTSNLHDFQ LNQSNLVLVS
GVVDYLKLFN PHDKTDYSMF EDIQDHVEFT YSSQRKHQWI DLSQFLKDID PIIKEYSDTY
KIAITDVKTR SWNKLPQQES VLQAAKLQVE YYRNMFGILA GEFDDIEIGY EMLLENAKRR
NLDVDKPISI KSALALLKAN HTIILKDYVK LANGEAIGFE SFDRFSQERY LNQGSEYDFT
KVLEGTNRED YISQIKASDK DGFDFDEILT SDILKAWKIP LTLRYFAARS SQLFHLCKPF
LSDSLSIEYH NVKKNDQCFH TNYYNYNANE IDEVTAKASA FWNGTRPPIP VQDLSKCNYC
DFSSRCVIPN PHKNVPGSYG SVGSKMKHFI
