ID A0A1R1PBW3_ZANCU Unreviewed; 436 AA.
AC A0A1R1PBW3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 03-MAY-2023, entry version 25.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN ORFNames=AX774_g8156 {ECO:0000313|EMBL:OMH78454.1};
OS Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX NCBI_TaxID=1213189 {ECO:0000313|EMBL:OMH78454.1, ECO:0000313|Proteomes:UP000188320};
RN [1] {ECO:0000313|Proteomes:UP000188320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL-18-3 {ECO:0000313|Proteomes:UP000188320};
RA Wang Y., White M., Kvist S., Moncalvo J.-M.;
RL Submitted (JAN-2017) 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|RuleBase:RU910737}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {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:OMH78454.1}.
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DR EMBL; LSSK01001923; OMH78454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1PBW3; -.
DR Proteomes; UP000188320; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd09908; H3TH_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; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
DR PANTHER; PTHR11081:SF8; EXONUCLEASE 1; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR Pfam; PF00867; XPG_I; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00842; XPG_2; 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|RuleBase:RU910737};
KW Excision nuclease {ECO:0000256|RuleBase:RU910737};
KW Exonuclease {ECO:0000256|RuleBase:RU910737, ECO:0000313|EMBL:OMH78454.1};
KW Hydrolase {ECO:0000256|RuleBase:RU910737};
KW Magnesium {ECO:0000256|RuleBase:RU910737};
KW Metal-binding {ECO:0000256|RuleBase:RU910737};
KW Nuclease {ECO:0000256|RuleBase:RU910737};
KW Nucleus {ECO:0000256|RuleBase:RU910737};
KW Reference proteome {ECO:0000313|Proteomes:UP000188320}.
FT DOMAIN 1..69
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 258..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 48747 MW; 232A73CBDCB4BA98 CRC64;
MGIEYLVAPY EADAQLAFLE KRGIVDFIIT EDSDMLAFGC KKVVFKLDDT GNGILFDREN
LKLVKTISLA TFTNESFRHM CILSGCDYLD SVHNVALKKA HKYLLQNKQI SKVVHLMRCD
GLNVPPDYLR MFDIADKTFL HQKVFDPIEK RLRHLEDLSE NVDSEILKYF GDLDDDEIAH
YIAIGEIDPS THRPFADSSC LENSTPKDNL LSRWIRPKPA LKGHSSEPIR KNPIFFHIYL
TSNRHLYSTH ILPIVHKSHG DHSKTTDKPP TPSYITPTNR TTTICTSSFR SFSRSPSVTS
SASSTTSSVT TTPTSNTISS FFSSSTSTST SKSMSLFPAN IPLGPKRLFS STSLTESRAG
LLTSDFQVKR RKSSIEPDTN RTEKLSRFFS SSILHTPSIK LSSTSKPING SRSSSINLSP
TESIKISSIL KHTKKP
//
