ID A0A1S3YMU3_TOBAC Unreviewed; 498 AA.
AC A0A1S3YMU3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-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 Name=LOC107777923 {ECO:0000313|RefSeq:XP_016453579.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016453579.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016453579.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000256|ARBA:ARBA00007092, ECO:0000256|RuleBase:RU362131}.
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DR RefSeq; XP_016453579.1; XM_016598093.1.
DR AlphaFoldDB; A0A1S3YMU3; -.
DR SMR; A0A1S3YMU3; -.
DR STRING; 4097.A0A1S3YMU3; -.
DR PaxDb; 4097-A0A1S3YMU3; -.
DR GeneID; 107777923; -.
DR KEGG; nta:107777923; -.
DR OMA; WPWISSE; -.
DR OrthoDB; 161558at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR CDD; cd09087; Ape1-like_AP-endo; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR020847; AP_endonuclease_F1_BS.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
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 Pfam; PF02037; SAP; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
DR PROSITE; PS50800; SAP; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU362131};
KW DNA repair {ECO:0000256|RuleBase:RU362131};
KW Lyase {ECO:0000313|RefSeq:XP_016453579.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2, ECO:0000256|RuleBase:RU362131};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2,
KW ECO:0000256|RuleBase:RU362131};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051}.
FT DOMAIN 46..80
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 84..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 391
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 393
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 463
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 489
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 498 AA; 55517 MW; 664349C9296B530F CRC64;
MGSKKRPFLT SSAIAKSNEP MGVAAEKGVS KENVDKEILV EDMETVEKMT VPQLRVKLRS
LGIPSRGTKQ ELVTSLKTFL DSKLNDAGNG SVAQEDQVSS EKSLGVVDNT SKRKARKVSS
NQRDVAASEV SSTRKTKKRV KEDNTKDTSA DIIVKQAEIT LGLSAESNDI KGKKTVRAKR
KVSSLTASAH IGVSEGVDIS VNQDEPWTIF AHKKPKDGWI VYNPKTMRPA PLSKDTKHVK
LLSWNVNGLR ALLKLKNLLI QQLADREDFD VLCLQETKLQ DKDVEAIKES LSGYENSFWT
CSVAKLGYSG TAIISRIKPL SVRYGLGIPD HDTEGRLVTV EFDNFYLLCG YVPNSGDGLR
RLTYRITEWD PSLGNYMKEL EKSKPVVLTG DLNCAHEEID IYNPAGNKRS AGFTEEERQS
FETNFLNKGF VDTFRKQHPG VVGYTYWGYR HGGRKTNKGW RLDYFLVSER IADNVHDSYI
LPDVDGSDHS PIGLILKL
//
