ID A0A0A2KCD8_PENIT Unreviewed; 370 AA.
AC A0A0A2KCD8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN ORFNames=PITC_093150 {ECO:0000313|EMBL:KGO64588.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO64588.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO64588.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO64588.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.; EC=3.2.2.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001668};
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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:KGO64588.1}.
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DR EMBL; JQGA01001571; KGO64588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KCD8; -.
DR STRING; 40296.A0A0A2KCD8; -.
DR HOGENOM; CLU_038423_0_1_1; -.
DR OMA; EKFPEHW; -.
DR OrthoDB; 276614at2759; -.
DR PhylomeDB; A0A0A2KCD8; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd08972; PF_Nei_N; 1.
DR Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR PANTHER; PTHR22993:SF9; ENDONUCLEASE 8-LIKE 1; 1.
DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Ribonucleoprotein {ECO:0000313|EMBL:KGO64588.1};
KW Ribosomal protein {ECO:0000313|EMBL:KGO64588.1}.
FT DOMAIN 2..132
FT /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51068"
FT REGION 292..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 41614 MW; 6E17E612C3171D44 CRC64;
MPELAEIHRI VHFIREHLVG KTLSKVQAQH DDIIFGKVGT SATEFQKAMQ GKKIVGAGQQ
GKYFWITMSS PPHAVMHFGM AGWLKIKDAD TYYYRTDKPA DQEWPPKYWK FLLETSEEPK
TEAAFVDARR LARIRLVDCP ADEIRNHTPL KENGPDPVAD KDTVNEAWLA EKLGKKKVPI
KALLLDQANI SGIGNWMGDE ILYHAKIHPE QYSNTLDADQ IKALHSAIHY VCSTSIGVLA
DSEKFPEHWL FKHRWGKGKK SQPAALPNGD KITFLTVGGR TSAVVPAVQK KTGPVAKDVD
EEVAKPTPAN SKRKRVALKK ESDSEEEQAT KTKQRDTPKR KNPTVKSENF EEEKPKPAVV
GRRRSTRTSK
//
