EXO5_YEAS1
ID EXO5_YEAS1 Reviewed; 585 AA.
AC B3LMZ5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
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=SCRG_02806;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408048; EDV11948.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LMZ5; -.
DR EnsemblFungi; EDV11948; EDV11948; SCRG_02806.
DR HOGENOM; CLU_019985_0_0_1; -.
DR Proteomes; UP000008335; 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 GO; GO:0000002; P:mitochondrial genome maintenance; IEA:InterPro.
DR InterPro; IPR016610; Exo5.
DR InterPro; IPR019190; EXOV.
DR PANTHER; PTHR14464; PTHR14464; 1.
DR Pfam; PF09810; Exo5; 1.
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; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..585
FT /note="Exonuclease V, mitochondrial"
FT /id="PRO_0000406691"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 552
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 558
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 585 AA; 67520 MW; F5F7B5BD3A599FF9 CRC64;
MLGRTLINKH GFLIHPRRFV HLNDKSLDGT FILPSKKNHM YDVPTNDPSG ILNASDIDRI
NNLPFFDNTS PTKETNTKEG ALLSEKLASV KELFGEDPEN PSFINYRFPR GLENPYFDIQ
VNQLKKKRLS VTQLCTTQNW CELRNFYDFY SQNLSNQLLN LKFQVQKGKK IHKSLEDETH
PELNQYKSFT HNFLALTKLS MDIDNDMDAL LDNWFNSINR LVSLFTKGDG HAREIVCHGF
INLEDGKLVE HLLNSDSKTK ENVIISGVID HLTLRNKHNH QVQKGAAHLD TEYQSWGNIL
TNLLSNLKEL KSNNEIVISD IKTRSVPKIP SIESVIESSK LQTMYYKFFF SHLSQDMTQT
YHSFLINAKR RGLDVDAPIN PTKILTFILT NPLFANDVKN LLYGLPINHS AFDNDAKGSN
TFDMAAFNDL LDRGPTSFNV PIEQDEDSSE STKCVSLRDY GHFYTKWKTP LTLKYFAARL
SQIYFIVGNL VSNDLMIEYY YHNDNFHNII FPYDTLKLGT HAHDSAMVWF GGRDMHPIEP
TQKNFNTYCK FCDYRHVCSW KNKNELKLID LGKELKKIIL ESSMK