EXO1_DICDI
ID EXO1_DICDI Reviewed; 1046 AA.
AC Q54ED2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Exonuclease 1;
DE EC=3.1.-.-;
GN Name=exo1; ORFNames=DDB_G0291570;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess
CC a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in
CC DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts
CC directed by strand breaks located either 5' or 3' to the mismatch. Also
CC exhibits endonuclease activity against 5'-overhanging flap structures
CC similar to those generated by displacement synthesis when DNA
CC polymerase encounters the 5'-end of a downstream Okazaki fragment (By
CC similarity). {ECO:0000250}.
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: Interacts with the mlh1-pms2 heterodimer via mlh1. Interacts
CC with msh3. Interacts with the msh2-msh6 heterodimer via msh2, and this
CC interaction may increase the processivity of the 5'->3' exonuclease
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61769.1; -; Genomic_DNA.
DR RefSeq; XP_635308.1; XM_630216.1.
DR AlphaFoldDB; Q54ED2; -.
DR SMR; Q54ED2; -.
DR STRING; 44689.DDB0232997; -.
DR PaxDb; Q54ED2; -.
DR EnsemblProtists; EAL61769; EAL61769; DDB_G0291570.
DR GeneID; 8628252; -.
DR KEGG; ddi:DDB_G0291570; -.
DR dictyBase; DDB_G0291570; exo1.
DR eggNOG; KOG2518; Eukaryota.
DR HOGENOM; CLU_291785_0_0_1; -.
DR InParanoid; Q54ED2; -.
DR OMA; MLRQMCI; -.
DR Reactome; R-DDI-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-DDI-5693607; Processing of DNA double-strand break ends.
DR PRO; PR:Q54ED2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:dictyBase.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; ISS:dictyBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:dictyBase.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; IMP:dictyBase.
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; IPR019734; TPR_repeat.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
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.
PE 3: Inferred from homology;
KW DNA damage; DNA excision; DNA repair; DNA-binding; Endonuclease;
KW Excision nuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..1046
FT /note="Exonuclease 1"
FT /id="PRO_0000328560"
FT REGION 1..99
FT /note="N-domain"
FT /evidence="ECO:0000250"
FT REGION 394..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..685
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 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1046 AA; 116366 MW; 7AD1618AC14E5C08 CRC64;
MGISGLLPAL SPVTKAIHVK DYANKRVAID GYSWLHKGAY SCSQEIVLGI PTRNYINYFI
SRIKMLISYK VIPVVIFDGG PLPNKKLKEQ ERLRHREEYK NKAKAYLLEG NKSQANICFQ
KAVDITPRMA FLLIKELRAL KVEYLVAPYE ADAQLTYLSI TGQVDAIITE DSDLVAFGAT
HIIFKMDKYG YAQEIKTEDL GSCKKDGYDF IDFNQTMLRQ MCILSGCDYL PSLSGMGLKT
SFKLLKQHRD IEKVFKYLKR EKSNFSQEYE QQFYKADFTF KHQRVFDPVS RILTTLLPLP
TIIDSRFLND NNNNTNDGDS NGDGSSGGSG SGGGFLDFIG PVIDDEIAEK IALGIIDPET
HEQFDKTQPY PKNTFTPQPK KLLSPISFNT KEFKNQTNNN NNNNNNIKSN NGTNNKNGMI
LNEGKLVQKG RNLNDQFTFA SNKITQYMTT TTTTTTTTTT TKNNNNNQKQ QPMIEDDTGY
DFQIDSFEID DCLNDDDDDE SIILSNNLNN QENVLESDCE FDDDDDQRGI DVDDSEKKDS
FVLDSDYEDE KEEEEVKSST FNSSSSISSG NSSKIKKTLV SSKFFVSSES SVLESDDDDG
GDDDDDSFNH NQNFSSSGNN IQPNSNIFHN GELSSYGYQK NQKNFKNVNS NSSSNSSNSS
NSSSGNSNSG NRIFNSGNSS NKNNTNGGIV KSTLLSSNDR VSLNFFDQFQ FDGKKKQSIL
VSQSRKSFSS PTLSNNEDYD SSFVSSTIPS SIGDDYDQMN SCSNNNNFNY NNSSNFNNNN
INNSNNNRNS GFSGFLKRKS SSQTAAPTTP TTPTTPKTSS SSSSTLTNST ITTEHSSYIL
KKPKYQATSN SPISTLDSSQ NYNDQSFISK KAHSFSSLDS DLIFKEDDVD NLIFNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNDNNNKIT TPSNKSFNSI
VLTTTSATTS ITQQDNEIYT TPKKKLPSTP ISSSSNDIIS KYFSSPSKVG PKSEGAPPTP
VNLEGMSLRS VLSLRYQQTM ASSPTK
