ID A0A0M3J251_ANISI Unreviewed; 347 AA.
AC A0A0M3J251;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 03-MAY-2023, entry version 29.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN ORFNames=ASIM_LOCUS1484 {ECO:0000313|EMBL:VDK18809.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0000160701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0000160701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK18809.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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|RuleBase:RU910737}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000256|RuleBase:RU910737}.
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DR EMBL; UYRR01001598; VDK18809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3J251; -.
DR WBParaSite; ASIM_0000160701-mRNA-1; ASIM_0000160701-mRNA-1; ASIM_0000160701.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
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.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW DNA excision {ECO:0000256|RuleBase:RU910737};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU910737};
KW DNA-binding {ECO:0000256|RuleBase:RU910737};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Excision nuclease {ECO:0000256|RuleBase:RU910737};
KW Exonuclease {ECO:0000256|RuleBase:RU910737};
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:UP000267096}.
FT DOMAIN 4..68
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
SQ SEQUENCE 347 AA; 39216 MW; FD781CB218D4D113 CRC64;
MDMVDILVAP YESDAQLAFL TQTGIAHAVV TEDSDLIAFG CEKIILKMQA DGSCTIYERS
ELPKCFSRPL CDDFDFTKFR RICILAGCDY LKNGLPGVGL NKAATFMSKT SGTNLEQILP
RLPRYLNMKN LKIKKEFIAD AIRAENTFLH QIVYDPRQRR QRPLNEYPKS DGTPEDEDFV
CITIDDENQT DYSYAGKIDS PTTAFRLVST YSDSDAQLNF KIRMALGNLA EQPRICDKFT
LPKEIPEWSI WSPNFRNGAE RLKARKEAEE AKKQMCGAFV LTGVRKVQRS STAIIYEKNA
RDDDTTVSGE EDEDDFIQPI QTKSNHAVNK NIKVNSLVSI SNTLICN
//
