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Database: UniProt
Entry: A0A2J7R5A2_9NEOP
LinkDB: A0A2J7R5A2_9NEOP
Original site: A0A2J7R5A2_9NEOP 
ID   A0A2J7R5A2_9NEOP        Unreviewed;       328 AA.
AC   A0A2J7R5A2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   RecName: Full=Exonuclease 1 {ECO:0000256|ARBA:ARBA00020324, ECO:0000256|RuleBase:RU910737};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
DE   Flags: Fragment;
GN   ORFNames=B7P43_G00579 {ECO:0000313|EMBL:PNF36018.1};
OS   Cryptotermes secundus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX   NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF36018.1, ECO:0000313|Proteomes:UP000235965};
RN   [1] {ECO:0000313|EMBL:PNF36018.1, ECO:0000313|Proteomes:UP000235965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:PNF36018.1};
RA   Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA   Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA   Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA   Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA   Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA   Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA   Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA   Bornberg-Bauer E.;
RT   "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL   Submitted (DEC-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:PNF36018.1}.
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DR   EMBL; NEVH01007392; PNF36018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J7R5A2; -.
DR   STRING; 105785.A0A2J7R5A2; -.
DR   InParanoid; A0A2J7R5A2; -.
DR   Proteomes; UP000235965; 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   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|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769,
KW   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:UP000235965}.
FT   DOMAIN          10..83
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          299..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         328
FT                   /evidence="ECO:0000313|EMBL:PNF36018.1"
SQ   SEQUENCE   328 AA;  37392 MW;  BA9BF5BF27479A70 CRC64;
     MALALIHECR RRNVDCIVAP YEADAQLAYL NLKNIAQIVI TEDSDLVLFG CTKILFKMDL
     AGNGLLVEQE HLHLAMGTRP EKFNFDKFRY MCILSGCDYL PSLPGIGLSK ACKFILRTAD
     TDIHRALSRL PAHLNMKSLT VSEDYRNHFL LADAAFKYQL VFDPLSRRLV HLNEPQGSEK
     VTDYAGKMLP SDTAYQLALG NLNPFTLQKV DDFNPDMVQQ RQNVKTNSWN QLSVAPHASI
     WSQGYKVPSV CLKQDPRQVD RPSTKGKLLK KEVSFVTQSK RHHDDVSDTC PDEDLTSMYF
     DMSVHEEPRK RRRSDSCELD EPEVEKEN
//
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