EXO1_XENLA
ID EXO1_XENLA Reviewed; 734 AA.
AC Q9W6K2; Q5XHF5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Exonuclease 1;
DE EC=3.1.-.-;
DE AltName: Full=Exonuclease I;
GN Name=exo1; Synonyms=exoi;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bibikova M., Carroll D.;
RT "Xenopus laevis homolog of ExoI.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also contain
CC a cryptic 3'->5' double-stranded DNA exonuclease activity. 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.
CC Required for DNA mismatch repair (MMR) (By 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 -!- 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; AF134570; AAD31867.1; -; mRNA.
DR EMBL; BC084102; AAH84102.1; -; mRNA.
DR RefSeq; NP_001083827.1; NM_001090358.1.
DR AlphaFoldDB; Q9W6K2; -.
DR SMR; Q9W6K2; -.
DR DNASU; 399140; -.
DR GeneID; 399140; -.
DR KEGG; xla:399140; -.
DR CTD; 399140; -.
DR Xenbase; XB-GENE-982081; exo1.S.
DR OMA; ATIGDLW; -.
DR OrthoDB; 796591at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 399140; Expressed in egg cell and 15 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0048256; F:flap endonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
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 2: Evidence at transcript level;
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..734
FT /note="Exonuclease 1"
FT /id="PRO_0000154042"
FT REGION 1..99
FT /note="N-domain"
FT REGION 138..229
FT /note="I-domain"
FT REGION 599..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
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"
FT CONFLICT 604
FT /note="P -> A (in Ref. 2; AAH84102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 734 AA; 82232 MW; 36288CAE9DA44611 CRC64;
MGIQGLLQFL KEASEPVHVK KYKGKTVAVD TYCWLHKGAF ACAEKLAKGE PTDQYVQFCM
KLVHMLLSFG VKPILVFDGC TLPSKKDVEK ARREKRQTNL QKGKQLLREG KLAEARECFS
RSVNITSSMA HEVIKAARSE GVDYIVAPYE ADSQLAYLNK NDFAEAIITE DSDLLAFGCK
KVLLKMDKFG NGLEIDQARF GMCRSLGDVF TEEKFRYMCI LSGCDYLPSI HGIGLAKACK
LLKVANNPDI TKVIQKIGQY LKTNITVPEG YIEGFLRANN TFLYQLVFDP VERKLIPLNP
YGNDVNPEEL NYAGPNMGDS VALQIALGNM DINTRKQIDD YNPDIPQLSH HRSQSWDNKQ
LNRKTAHTDS IWYTKSEPCK TTKIEEIHSP RGLILPSKKH TVKRSYEDGV SDTDLISQYS
FSKNKKARPD GDDPMQQVPA STMILQPLDD CANTKPKKPI HQPKTRNAFA TFLQRQKQDC
SSVSATGTRS RFFYKPADEK PHCTEKEQIV CNGSALDIAK ETHELTEESS IKTEKEDSLS
TISEVCKPNN QRISPLQNQR SCFTWSGSLD SESSPTPKQS PMLLSLQKFH RTTPYMQNEA
ENKPSWQSSC IKSDTVSQID SNEKLLKKQD IEDTDSDEHA STPESPCQFT MKASPAHQSF
FPEPKGSAPK SKVPGLLKSQ SVVSGLRTKV KPRAPAKVSG LTNRSNTKAT RNNENVPGLQ
ATIGDLWKNF SYKK
