EXO5_YEAST
ID EXO5_YEAST Reviewed; 585 AA.
AC P38289; D6VQF9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=YBR163W; ORFNames=YBR1215;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=10628851; DOI=10.1007/pl00013817;
RA Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H.,
RA Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G., Kramer W.,
RA Klein S., Koetter P., Kricke J., Launhardt H., Mannhaupt G., Maierl A.,
RA Meyer P., Mewes W., Munder T., Niedenthal R.K., Ramezani Rad M.,
RA Roehmer A., Roemer A., Rose M., Schaefer B., Siegler M.-L., Vetter J.,
RA Wilhelm N., Wolf K., Zimmermann F.K., Zollner A., Hinnen A.;
RT "Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by
RT a systematic approach.";
RL Mol. Gen. Genet. 262:683-702(1999).
RN [4]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3286646; DOI=10.1016/s0021-9258(18)68447-9;
RA Burgers P.M., Bauer G.A., Tam L.;
RT "Exonuclease V from Saccharomyces cerevisiae. A 5'-3'-deoxyribonuclease
RT that produces dinucleotides in a sequential fashion.";
RL J. Biol. Chem. 263:8099-8105(1988).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-270 AND ASP-320.
RX PubMed=20086101; DOI=10.1128/mcb.01321-09;
RA Burgers P.M., Stith C.M., Yoder B.L., Sparks J.L.;
RT "Yeast exonuclease 5 is essential for mitochondrial genome maintenance.";
RL Mol. Cell. Biol. 30:1457-1466(2010).
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.
CC {ECO:0000269|PubMed:10628851, ECO:0000269|PubMed:20086101,
CC ECO:0000269|PubMed:3286646}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3286646};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:3286646};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20086101}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z36032; CAA85123.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07279.1; -; Genomic_DNA.
DR PIR; S46034; S46034.
DR RefSeq; NP_009722.3; NM_001178511.3.
DR AlphaFoldDB; P38289; -.
DR BioGRID; 32863; 34.
DR IntAct; P38289; 3.
DR MINT; P38289; -.
DR STRING; 4932.YBR163W; -.
DR MaxQB; P38289; -.
DR PaxDb; P38289; -.
DR PRIDE; P38289; -.
DR EnsemblFungi; YBR163W_mRNA; YBR163W; YBR163W.
DR GeneID; 852461; -.
DR KEGG; sce:YBR163W; -.
DR SGD; S000000367; EXO5.
DR VEuPathDB; FungiDB:YBR163W; -.
DR eggNOG; ENOG502QR0P; Eukaryota.
DR GeneTree; ENSGT00390000015205; -.
DR HOGENOM; CLU_019985_0_0_1; -.
DR InParanoid; P38289; -.
DR OMA; LQVMYYR; -.
DR BioCyc; YEAST:G3O-29113-MON; -.
DR PRO; PR:P38289; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38289; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR InterPro; IPR016610; Exo5.
DR InterPro; IPR019190; EXOV.
DR PANTHER; PTHR14464; PTHR14464; 1.
DR Pfam; PF09810; Exo5; 1.
DR PIRSF; PIRSF013220; UCP013220; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA-binding; Exonuclease; Hydrolase; Iron; Iron-sulfur; Magnesium;
KW Metal-binding; Mitochondrion; Nuclease; Reference proteome;
KW 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_0000202501"
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"
FT MUTAGEN 270
FT /note="D->A: Impairs exonuclease activity."
FT /evidence="ECO:0000269|PubMed:20086101"
FT MUTAGEN 320
FT /note="D->A: Impairs exonuclease activity."
FT /evidence="ECO:0000269|PubMed:20086101"
SQ SEQUENCE 585 AA; 67570 MW; 92DBE35B819E0AFB CRC64;
MLGRALINKY 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 HLTLRNRHNH QVQKGAAHLD TEYQSWGNIL
TNLLSNLKEL KSNNEIVISD IKTRSVPKIP SIESVIESSK LQTMYYKFFF SHLSQDMTQT
YHSFLINAQR RGLDVDAPIN PTKILTFILT NPLFANDVKN LLYGLPINHS AFDNDAKGSN
TFDMTAFNDL LDRGPTSFNV PIEQDEDSSE STKCVSLRDY GHFYTKWKTP LTLKYFAARL
SQIYFIVGNL VSNDLMIEYY YHNDNFHNII FPYDPLKLGT HAHDSAMVWF GGRDMHPIEP
TQKNFNTYCK FCDYRHVCSW KNKNELKLID LGKELKKIIL ESSMK
