ID A0A0B7FY48_THACB Unreviewed; 559 AA.
AC A0A0B7FY48;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease {ECO:0000256|RuleBase:RU362131};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU362131};
GN ORFNames=RSOLAG1IB_04559 {ECO:0000313|EMBL:CEL61809.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL61809.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL61809.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL61809.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) 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}.
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DR EMBL; LN679105; CEL61809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7FY48; -.
DR STRING; 1108050.A0A0B7FY48; -.
DR Proteomes; UP000059188; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase 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 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 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:CEL61809.1};
KW Hydrolase {ECO:0000313|EMBL:CEL61809.1};
KW Lyase {ECO:0000313|EMBL:CEL61809.1};
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:CEL61809.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000059188};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 490..551
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 383..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 155
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 157
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 230
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 256
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 559 AA; 62520 MW; 3ABE1FAB3A5ED74D CRC64;
MKISRQLLTR SMAVPESYDA VMSFPKSKGG YSGVAVYTHS AKVVPLKAEE GLIGGYQSTS
KITMDAQDRI SKAYPKPSSL ELMPEEGGVP TELNDLDSEG RSLVVDFGLF VLINVYCPNL
TSEERMPFKY NFHKVLEDRV RILIQEGREV IVLGDMNVVA APIDHCEGVL DSRKNTFWDS
PVRTWFRQWL DPEGPMIDAI RSSWPDREKM FTCWDTRTNA RESNYGTRID YILITRGLLP
WFKYGDIQPD IRGSDHCPLF IDLHDEITTP DGQTLRLADF LDTPGDSGQH RDPPPTSTKF
WDEFSGKQKL LSTFFAKKSA QSTSELPIPT PKLDRQEVVP ESGIQKDALA SVDPVSICST
QTYSPIVGHS KVGQSTEVDV RKRKTIGSNS ETSSSNFKKS KKSQITNVVN GQHKLSNFFT
NPSQLGSSTK RSISPPIEII DSEDEDKTSN TVNELLLSGS SSALSSQPKD TSSTKQAWSQ
LMRPIEPPKC TVHNAPTKEF AVNKPGPNKG KKFFICSMPM GPGYDSGKST RLREEVDPRY
RCNYFKWASD VKRETKAKD
//