EXO5_PICST
ID EXO5_PICST Reviewed; 573 AA.
AC A3M0E6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 58.
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=PICST_64329;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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=ABN68512.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000502; ABN68512.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001386541.2; XM_001386504.1.
DR AlphaFoldDB; A3M0E6; -.
DR STRING; 4924.XP_001386541.2; -.
DR EnsemblFungi; ABN68512; ABN68512; PICST_64329.
DR GeneID; 4840960; -.
DR KEGG; pic:PICST_64329; -.
DR eggNOG; ENOG502QR0P; Eukaryota.
DR HOGENOM; CLU_019985_0_0_1; -.
DR InParanoid; A3M0E6; -.
DR OrthoDB; 1601909at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
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; 2.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..573
FT /note="Exonuclease V, mitochondrial"
FT /id="PRO_0000285325"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 573 AA; 65941 MW; D5F7E0B1489E24FF CRC64;
MRAKSILKQF LLPRDKNSSE VGKSDSIELF PNDSLHSLYA NWHLPGSHML PLYNPTNISP
YEFHSRFNSD QSYKRSPRLS VTKLLTDRWC ELSEYYTIYA GSPQFKVTNA ITQGLERHSE
LEYELHQPID ISLLMETLSG SISDAISHFQ ATIKDVKDPD LLSELDGNPD AAKLAMEWSD
HSINRLFSLI TTSEAREVLV HGFLNLENSE FVSSIDELKN SQNGNIDIRK VLVSGIVDHF
KIENLEDPTD LSLFREIRDY MDYYFDTTIG DKQVIDLTKF LQSVKQFVEE HKSAFSVKTT
DVKTRSVNRL PSSISVLEAA KFQTFYYRKM FGLLSNEHQR TENNHFAYYS LLENARVRGI
DVDEPLDIVT LVSILRKNYN LFYLDFVKLA NGEPIGFEPF DSYNKGRENT GFALDSVFGI
AEKCLLAGKP MQLDLIEKIN SLEDFNYDEI LSPDLIKNWK TAPTLRYLAA RCAQFYELFS
ELLGDHTAVE YHNGRTSQAF HTSESKYTED VIGEQTRKAS TFWNGKRFPI YTRDLSKCNY
CDFKPRCMVP NHQLQGDLYR KSLGAKINEF LHS