ID A0A074S711_9AGAM Unreviewed; 597 AA.
AC A0A074S711;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease {ECO:0000256|RuleBase:RU362131};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU362131};
GN ORFNames=V565_007120 {ECO:0000313|EMBL:KEP55206.1};
OS Rhizoctonia solani 123E.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP55206.1, ECO:0000313|Proteomes:UP000027456};
RN [1] {ECO:0000313|EMBL:KEP55206.1, ECO:0000313|Proteomes:UP000027456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=123E {ECO:0000313|EMBL:KEP55206.1,
RC ECO:0000313|Proteomes:UP000027456};
RA Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA Zafar N., Nierman W.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2,
CC ECO:0000256|RuleBase:RU362131};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2,
CC ECO:0000256|RuleBase:RU362131};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR604808-2, ECO:0000256|RuleBase:RU362131};
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, ECO:0000256|RuleBase:RU362131}.
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:KEP55206.1}.
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DR EMBL; AZST01000009; KEP55206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074S711; -.
DR STRING; 1423351.A0A074S711; -.
DR HOGENOM; CLU_010374_2_1_1; -.
DR OrthoDB; 169291at2759; -.
DR Proteomes; UP000027456; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd09088; Ape2-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 InterPro; IPR010666; Znf_GRF.
DR NCBIfam; TIGR00633; xth; 1.
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 SUPFAM; SSF56219; DNase I-like; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU362131};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU362131};
KW Endonuclease {ECO:0000313|EMBL:KEP55206.1};
KW Hydrolase {ECO:0000313|EMBL:KEP55206.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2, ECO:0000256|RuleBase:RU362131};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604808-2}; Nuclease {ECO:0000313|EMBL:KEP55206.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000027456};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 528..589
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 401..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
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 299
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
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 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 299
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 273
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 299
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 597 AA; 66902 MW; F5CA121E4DF16F7F CRC64;
MRILSWNVNG IRTLSQYHPW YTLKTCEEML KELGADIICF QEMKISRQLL TKTLAVPENY
DAVMSFPRNK NGYSGVAVYT NNSKVVPLKA EEGLVGGYQQ TSRVTLDAKE RISETYPESS
VLELMAEEEG GVPTDLDSLD SEGRCLVVDF GLFVLINVYC PNLTSEERMA FKYNFHKVLQ
DRVRILIQEG REVICLGDLN VVASPIDHCE GSLESRKNTF WESPVRTWFR EWLDPEGPMV
DVVRNSWPDR EKMFTCWDTR TNARESNYGT RIDYILITRG LLPWFKHGDI QPDIRGSDHC
PIFIDLHDEI TLPDGQTSRL VDVLGSCSAS GQRRDPPPIS TKFWNEFSGK QKLLSMFFAK
KSQSTSKPLI PGPEGSSQEI TTGRGTVKGE LSCDQPVLTS TIQIRLPSPG RSEPQQSAGV
DGRKRKAVRS NEETSSFGSK KSKKSQIAGG VGKQPKLSNF FASSQLGNSQ RSSSPIELSD
SEVEVEISKS TSELLSGSNP SLCSQTKDPS LAKDAWSHIM RPIEPPRCNV HDILTKELTV
NKAGPNKGKK FFICSMPMGP GYDSGKSTRL REEVDPRYRC NYFKWASDVK RETKSAS
//
