ID S7QBG8_GLOTA Unreviewed; 561 AA.
AC S7QBG8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease {ECO:0000256|RuleBase:RU362131};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU362131};
GN ORFNames=GLOTRDRAFT_75533 {ECO:0000313|EMBL:EPQ56703.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ56703.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ56703.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ56703.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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 ---------------------------------------------------------------------------
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; KB469300; EPQ56703.1; -; Genomic_DNA.
DR RefSeq; XP_007865384.1; XM_007867193.1.
DR AlphaFoldDB; S7QBG8; -.
DR STRING; 670483.S7QBG8; -.
DR GeneID; 19308521; -.
DR KEGG; gtr:GLOTRDRAFT_75533; -.
DR eggNOG; KOG1294; Eukaryota.
DR HOGENOM; CLU_010374_2_0_1; -.
DR OMA; SFWICPR; -.
DR OrthoDB; 169291at2759; -.
DR Proteomes; UP000030669; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
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 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 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 533..561
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 357..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..444
FT /note="Polar 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 561 AA; 61361 MW; 444B7526F7849E8B CRC64;
MRILSWNING VRTLPQYHPW NTFKTFEGIL DELKADIICF QEMKTSRASL QPSAALPGRF
DAFFSFPANK GGYSGVAVYT DSRTVVPLKA EEGLSGRIQP ALKPPLAPAE RISAAYPQAH
ELALFTDAPD RTPTDPGALD AEGRALALDV GLFVLVNVYC PNETSDARLP FKMDFHRMLQ
ARVAQLIGER REVVVVGDMN ICAAPLDHCD GHLPSHASVF YDHPARRWFR DWLAPNGPMV
DAVREFWPER DGMYTVWNMK LCARETNYGT RVDYILTTPG LTKWLKGGNT LPSVKGSDHC
PIYVDLHDEI TLESGEVVKL RDAMQFGTRT EPPRLASKFW PEYSGKQKLL SSFFSKGGTD
TISKSPSPPQ LKASSPSTII GPSRSTQPLP PPPTASSSKS SIKPSPSPST SHPSRPLKRK
SSGPQSAETS SSNSTSQSKK RKPGQAKLSS FFTKPPAKSA SSLEVVVVDD DNDDPEGGGT
EHQLHADYLL ACELSASQQD LVEQSAEAGQ DKGKGKGKEA WSQLFAPVAP PKCTIHREPA
KLFTVNKPGP NKGKTFYICS R
//
