ID A0A329RUN2_9STRA Unreviewed; 719 AA.
AC A0A329RUN2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN ORFNames=PC110_g15403 {ECO:0000313|EMBL:RAW28225.1};
OS Phytophthora cactorum.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW28225.1, ECO:0000313|Proteomes:UP000251314};
RN [1] {ECO:0000313|EMBL:RAW28225.1, ECO:0000313|Proteomes:UP000251314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10300 {ECO:0000313|EMBL:RAW28225.1,
RC ECO:0000313|Proteomes:UP000251314};
RA Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU910737}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU910737};
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:0000256|RuleBase:RU910737};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU910737}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000256|ARBA:ARBA00010563,
CC ECO:0000256|RuleBase:RU910737}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAW28225.1}.
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DR EMBL; MJFZ01000505; RAW28225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329RUN2; -.
DR STRING; 29920.A0A329RUN2; -.
DR Proteomes; UP000251314; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09908; H3TH_EXO1; 1.
DR CDD; cd09857; PIN_EXO1; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
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; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081:SF8; EXONUCLEASE 1; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 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; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU910737};
KW DNA excision {ECO:0000256|RuleBase:RU910737};
KW DNA repair {ECO:0000256|RuleBase:RU910737};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU910737};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881,
KW ECO:0000256|RuleBase:RU910737};
KW Exonuclease {ECO:0000256|RuleBase:RU910737, ECO:0000313|EMBL:RAW28225.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU910737};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU910737};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU910737};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU910737};
KW Nucleus {ECO:0000256|RuleBase:RU910737};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000251314}.
FT DOMAIN 1..99
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 138..208
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 329..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 80223 MW; D58164EBB94308B3 CRC64;
MGISGLLPVL KSITETKNIE EYKGRTLAID GYCWLHRAIY SCSQEICLGQ ETDKYVTYFM
ARITALLHNG VTPYVVFDGG PLPMKKGTEE ERRKSRQKNR ELGIQHYNNK RFGEARKCFV
RAADVSPCMA HRVIQHLKAQ NVAYVVAPYE ADAQLAYLVK NGLADGVITE DSDCLPFGCQ
TVLFKMDRDN VAQEIQTVNL KKNKGMGFHM FTEQMFLEMC IFSGCDYLPS IPGFGLKKAY
TAMKQHGSFT KIIRALRLEG KTRVPATYEE GFRKAVLTFR HQRVYCPTKK EIVPLTPIPA
NQLETDPAMD FVGPMLPSDV AKAIADGDMD PTTMTPFPAR APLPSRNSSP AKSMIPSTRK
LTTAPNPKAA ITSFFHASES AAAAVFNTPR SKPTPTKRKL PPSFMDKWAS NATSPKEKSA
QSTVPDSVAK PATESPLVTS RFFGVKPKKM SPPDEYVKKS MPRTLDSLST FQSQEPRGAV
GARNISFDPL NDKVRVLPTA RDKVFSKENQ APNYQKATPS PPVPTKETAF SRMMRAGSML
QQHRLKKRKS IFRSGKPRIV ISSLTSVLMP RTKITWALLA KGQSTYDSDM LLESLYVVKK
SEISPCSLCT EPTPHNMRTR LLHCKCKACK AVAPYASCPW KGKTQTCILS NVVSISEPGQ
HVSPLRPPHR PRLTEEMKAF VRDMCTYNHK PMNIYNGIAR RFQVAESAMP TLAIVQRFV
//
