ID A0A3Q0J3B3_DIACI Unreviewed; 1056 AA. AC A0A3Q0J3B3; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 29-MAY-2024, entry version 22. DE RecName: Full=exodeoxyribonuclease III {ECO:0000256|ARBA:ARBA00012115}; DE EC=3.1.11.2 {ECO:0000256|ARBA:ARBA00012115}; GN Name=LOC108251834 {ECO:0000313|RefSeq:XP_026682906.1}; OS Diaphorina citri (Asian citrus psyllid). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae; OC Diaphorininae; Diaphorina. OX NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026682906.1}; RN [1] {ECO:0000313|RefSeq:XP_026682906.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (FEB-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield CC nucleoside 5'-phosphates.; EC=3.1.11.2; CC Evidence={ECO:0000256|ARBA:ARBA00000493}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Note=Probably binds two magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR604808-2}; CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|ARBA:ARBA00007092}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_026682906.1; XM_026827105.1. DR AlphaFoldDB; A0A3Q0J3B3; -. DR STRING; 121845.A0A3Q0J3B3; -. DR PaxDb; 121845-A0A3Q0J3B3; -. DR KEGG; dci:108251834; -. DR OrthoDB; 161558at2759; -. DR Proteomes; UP000079169; Unplaced. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:TreeGrafter. DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:TreeGrafter. DR GO; GO:0006284; P:base-excision repair; IEA:TreeGrafter. DR CDD; cd09087; Ape1-like_AP-endo; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR NCBIfam; TIGR00195; exoDNase_III; 1. DR NCBIfam; TIGR00633; xth; 1. DR PANTHER; PTHR22748; AP ENDONUCLEASE; 1. DR PANTHER; PTHR22748:SF6; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 3: Inferred from homology; KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2}; KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000079169}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..1056 FT /note="exodeoxyribonuclease III" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5018152902" FT DOMAIN 773..1047 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" FT REGION 307..326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 421..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 539..571 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 480..501 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 554..571 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 912 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 951 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 1047 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT BINDING 776 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 804 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 951 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 953 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 1046 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 1047 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 953 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 1021 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 1047 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" SQ SEQUENCE 1056 AA; 120817 MW; EA8491196BCB1610 CRC64; MDLFRLGNEV IVLVLDLLCV YCTLVSDNSS VPCLIQDNGA ILSSKPPFPS LKYSYSTFRW NETRPTTMFV TINRRHEYDF LYSDRECQVV RKKRVSPSRE MHLKDILATF DSEDGAIVVD ASRRDRKELK EPTLPEDLFD DLECESLHVS ELKDENDENI GAQSQVIHDS LFKHRNRTES HSPEPLKMTN PREDYDFFSD FNVKPIRKTS ANKSVKADDL KNVLNLFASE DGGYVPVLKK SVEISQEKEP TLPAILMGNS ELHVSEMEEN NDDSNIKLHR EVKSDVNEDQ ESNIKIVRDL DSEVINSEQT VDRTESSEDK YSKSQHGDLN DIYFPSNLYH KKTFKTTAGS SENILLKGLL MNRKSTQPRH SISTSKNRSP TQNEIDMIVE NFISVQRKFS LNTVRPVTHF LNVSNEESYE KYTFRKRKGK TKTTRIKTTK YSDKSTKRRG RPKKTTTPSG GIISSPSKNT RKHDKKYTTN SESIQTSVSN IRDSTSRNLK TKSVNIEDKS ESASTATLKT IGKEDKDFIS RPVKSSRVST KIQLDHSVKK SQKQGLTKYE SQPSSTSTST DVLPAHKMSL APERKIAQFN NRNKLVLLHT KTTHVKTVPS ENVQNTKGKF ELLKEIKFER TGSEDTSEDV EESGFFTVEP IPDSNLYNEW EYRPPKRKVK TSTFSLKSLK NLDDKLSYIR EVCGEHMPVN VTKKASRKNV FSFKLNEIHV GTGKIENRLG CDSSNETSYA EVEEVPIIDF NDPFRILEHK RRQDQYPWNF KIGSWNVNGI RAWSQKDGFS FMRQHDLNVF CIQEIRCPLE KLPECPEGYH AFWFPGTRQG YAGVAVLSKT KPVRVTHGFS MKVGGVVHTH GFNRGSNEHG SDMESGPSHP ELTTIQYADA SGIDDGRVMT VEYEQFYLVN VYAPAAKEDL SMLSVKLLWN SFLRGHLKSL NEIKPVVLAG DLNVAHNHID VALPLTNLGK SGFTIQERNY FSNFLDLGFL DVHRHLYPNH RIYTYWPYYD RPSKMKGWRL DYFLISKQLK SHLSDLEIHG DVEGSDHAPQ ILYLNL //