EXO1_SCHPO
ID EXO1_SCHPO Reviewed; 571 AA.
AC P53695;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Exodeoxyribonuclease 1;
DE EC=3.1.-.-;
DE AltName: Full=Exodeoxyribonuclease I;
DE Short=EXO I;
DE Short=Exonuclease I;
GN Name=exo1; ORFNames=SPBC29A10.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 139-160.
RC STRAIN=972 / ATCC 24843;
RX PubMed=7855597; DOI=10.1126/science.7855597;
RA Szankasi P., Smith G.R.;
RT "A role for exonuclease I from S. pombe in mutation avoidance and mismatch
RT correction.";
RL Science 267:1166-1169(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1737756; DOI=10.1016/s0021-9258(19)50688-3;
RA Szankasi P., Smith G.R.;
RT "A DNA exonuclease induced during meiosis of Schizosaccharomyces pombe.";
RL J. Biol. Chem. 267:3014-3023(1992).
CC -!- FUNCTION: 5'->3' double-stranded DNA exonuclease that could act in a
CC pathway that corrects mismatched base pairs.
CC {ECO:0000269|PubMed:1737756}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1737756}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: By meiosis.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000305}.
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DR EMBL; L35174; AAC41648.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22433.1; -; Genomic_DNA.
DR PIR; T43288; T43288.
DR RefSeq; NP_596050.1; NM_001021961.2.
DR AlphaFoldDB; P53695; -.
DR SMR; P53695; -.
DR BioGRID; 276877; 89.
DR STRING; 4896.SPBC29A10.05.1; -.
DR iPTMnet; P53695; -.
DR MaxQB; P53695; -.
DR PaxDb; P53695; -.
DR PRIDE; P53695; -.
DR EnsemblFungi; SPBC29A10.05.1; SPBC29A10.05.1:pep; SPBC29A10.05.
DR GeneID; 2540348; -.
DR KEGG; spo:SPBC29A10.05; -.
DR PomBase; SPBC29A10.05; exo1.
DR VEuPathDB; FungiDB:SPBC29A10.05; -.
DR eggNOG; KOG2518; Eukaryota.
DR HOGENOM; CLU_008978_5_1_1; -.
DR InParanoid; P53695; -.
DR OMA; CKAPTEQ; -.
DR PhylomeDB; P53695; -.
DR Reactome; R-SPO-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR PRO; PR:P53695; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0051908; F:double-stranded DNA 5'-3' exodeoxyribonuclease activity; IDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:PomBase.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:PomBase.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; TAS:PomBase.
DR GO; GO:0000710; P:meiotic mismatch repair; IMP:PomBase.
DR GO; GO:0006298; P:mismatch repair; IGI:PomBase.
DR GO; GO:0006312; P:mitotic recombination; TAS:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; TAS:PomBase.
DR CDD; cd09908; H3TH_EXO1; 1.
DR CDD; cd09857; PIN_EXO1; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR032641; Exo1.
DR InterPro; IPR037315; EXO1_H3TH.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR044752; PIN-like_EXO1.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; PTHR11081; 1.
DR PANTHER; PTHR11081:SF8; PTHR11081:SF8; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA damage; DNA repair; DNA-binding;
KW Excision nuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..571
FT /note="Exodeoxyribonuclease 1"
FT /id="PRO_0000154044"
FT REGION 1..96
FT /note="N-domain"
FT REGION 114..245
FT /note="I-domain"
FT REGION 464..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 571 AA; 63867 MW; 7D21B3778104BA9D CRC64;
MGIKGLLGLL KPMQKSSHVE EFSGKTLGVD GYVWLHKAVF TCAHELAFNK ETDKYLKYAI
HQALMLQYYG VKPLIVFDGG PLPCKASTEQ KRKERRQEAF ELGKKLWDEG KKSQAIMQFS
RCVDVTPEMA WKLIIALREH GIESIVAPYE ADAQLVYLEK ENIIDGIITE DSDMLVFGAQ
TVLFKMDGFG NCITIRRNDI ANAQDLNLRL PIEKLRHMAI FSGCDYTDGV AGMGLKTALR
YLQKYPEPRA AIRAMRLDKS LKVPVSFEKE FALADLAFRH QRVYCPKDKT LVHLSPPERE
LSVHEDAFIG SFFDNQLAID IAEGRSNPIT KCAFDIKDSS MQSFTKTTIT ISKRKGISKT
DISNFFMKSI PPSKRPTKST SLIDVTNVKV QRTHLANDIS SEKQSIKSAN EKAYVTPKSN
SLKPGFGKSL SDISNSATKN ENVPFLPPRT GVSKYFKLQK NTEKEIDEQV PSQSNNTTPT
SAKSDSASPQ NWFSSFSYQT PNSASPPFSS LSHTLPISAL AKIGHDALNR KNHASLPSRR
IVYKPPSSPS TPISMNPRPK GILSLQQYKF R
