ID A0AA88VDJ2_9ASTE Unreviewed; 890 AA. AC A0AA88VDJ2; DT 27-MAR-2024, integrated into UniProtKB/TrEMBL. DT 27-MAR-2024, sequence version 1. DT 24-JUL-2024, entry version 3. DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease 2 {ECO:0000256|ARBA:ARBA00013541}; GN ORFNames=RJ639_016418 {ECO:0000313|EMBL:KAK3006640.1}; OS Escallonia herrerae. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Escalloniales; Escalloniaceae; Escallonia. OX NCBI_TaxID=1293975 {ECO:0000313|EMBL:KAK3006640.1, ECO:0000313|Proteomes:UP001188597}; RN [1] {ECO:0000313|EMBL:KAK3006640.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCBG64.0493 {ECO:0000313|EMBL:KAK3006640.1}; RC TISSUE=Leaf {ECO:0000313|EMBL:KAK3006640.1}; RA Chanderbali A., Dervinis C., Anghel I., Soltis D., Soltis P., Zapata F.; RT "Draft genome assemblies for two species of Escallonia (Escalloniales)."; RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases. 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 -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|ARBA:ARBA00007092}. 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:KAK3006640.1}. 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 EMBL; JAVXUP010001965; KAK3006640.1; -; Genomic_DNA. DR Proteomes; UP001188597; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. 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:0008081; F:phosphoric diester hydrolase activity; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IEA:TreeGrafter. DR CDD; cd16461; RING-H2_EL5-like; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR InterPro; IPR010666; Znf_GRF. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR22748; AP ENDONUCLEASE; 1. DR PANTHER; PTHR22748:SF4; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE 2; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR Pfam; PF06839; zf-GRF; 1. DR Pfam; PF13639; zf-RING_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. DR PROSITE; PS51999; ZF_GRF; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2}; KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR604808-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP001188597}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00175}. FT DOMAIN 568..617 FT /note="GRF-type" FT /evidence="ECO:0000259|PROSITE:PS51999" FT DOMAIN 804..847 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT ACT_SITE 157 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 198 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 327 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT BINDING 198 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 200 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 326 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 327 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 200 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 269 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 327 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" SQ SEQUENCE 890 AA; 98868 MW; 702B2925C0080655 CRC64; MNEDCDLQRQ QSEEPHFTVR FPPTITPFLG CRYHLLSAKQ ELRADVVWAD GFESFFSCTR TVDRGRTGYS GVATFCRVKS AFSSNEVALP VDAEEGFTGL LENARGFGTR KDEFPNVAEG LEEFSREVLL KVDSEGRCII TDHGHFVSKL AVLFNIYGPR AECDDTERIQ FKHTFFKILQ RRWESLLHRG RRILVVGDLN IAPAAIDRCD AGSDFEKNEF RKWFRSLLVE NGGSFFDVFR AKHPERREAY TCWPTNTGAE EFNFGTRIDH ILIAGSCLHE VHNLEGHDFV TCHVAECNIL TQFKRWKPGN TPRWKGGRSI KLEGSDHAPV CISLFEIPNI PQHSTPSFST RYCPQVEGCQ QTLVSMLMRR QSAAKVNTTG GSSSSDEKVV VQSCNQSVKS SVEAYKLSGK SLDQPRPTED SASVTDECSQ ASFHDVSNKM LLNLGNNNTK QMRCVYPNKK ARHSQSSQLS LTSFFQKTSK CTGGDHSSDA VISLNQADLS SSNHYSGIAS MNDDESVILE KSDLNICASS QNLVEFDACQ SSEKEKRSVA LLEWQRIQQH MQSSIPLCKG HGESCVSRIV KKEGPNSGRR FYVCARAEGP ASNPEANCGY FKWADLRSKR KGRQFSLLVP AVLNMKHFGK QADLGYADLV LGREVDLVSL SKRQLVEDAK LALDKQDLNC LAPIVFDIKH LVGNLDSCLV KQASRALSFL LDSPPSPPPL AQPPLEVHHG YSEERTLYIS LGVLVKVALI SFLLNSLFCC SRRQSPNGVA RAVASNDTQV TAYDSSAPSP LSSASSRLVE SESCSICLAE FERGELLRVL PRCKHMFHKD CIDQWLPSRS LHCPVCRDCA IERDVKSGES CSSNTGTPAA NSSDLLVLTF ASTVHMPAHL //