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Database: UniProt
Entry: A0A0A2KP20_PENIT
LinkDB: A0A0A2KP20_PENIT
Original site: A0A0A2KP20_PENIT 
ID   A0A0A2KP20_PENIT        Unreviewed;       514 AA.
AC   A0A0A2KP20;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=DNA glycosylase {ECO:0000313|EMBL:KGO69597.1};
GN   ORFNames=PITC_000150 {ECO:0000313|EMBL:KGO69597.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO69597.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO69597.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO69597.1,
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   -!- 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:KGO69597.1}.
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DR   EMBL; JQGA01001132; KGO69597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KP20; -.
DR   STRING; 40296.A0A0A2KP20; -.
DR   HOGENOM; CLU_012862_9_3_1; -.
DR   OMA; DGCVIDH; -.
DR   OrthoDB; 5482962at2759; -.
DR   PhylomeDB; A0A0A2KP20; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0000702; F:oxidized base lesion DNA N-glycosylase activity; IEA:UniProt.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProt.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   PANTHER; PTHR47203; -; 1.
DR   PANTHER; PTHR47203:SF1; HYPOTHETICAL BASE EXCISION DNA REPAIR PROTEIN (EUROFUNG); 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   DOMAIN          229..435
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   REGION          16..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..514
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  55755 MW;  F035F2DB8DB66204 CRC64;
     MERRITRSAT RAAAALIAGE ENSPSVTQVP NTTKANKRKR LNPPTGNSNF PNALNTPKIN
     SITELKSCND FNPTIKPEKP LLPPASFNEF PHNLGSVLAP FSIATESKTS IAGSDKENQT
     VKGNQVTNLA TELQDTVNKA TTKLKKEPKI QTTPTGPKLK KNTYGLTPGI SPFPELVRPT
     AEECEDVNQL LSSIHGVVTA PATIPEPSLT VTGCGEVPSV LDALIRTLLS GATTGNNAAK
     AFGGLVQRFG VLSEGIGKGS VNWDAVRQAT VKDVFEAIKS GGLADIKSKN LKAILDIVHE
     DNQARRATLL DSESKNDAMS KLVPEKAEKD KQYEIACADQ NFLSLNHLHN LSTEEAMTNL
     IKYPGIGPKT AACVILFCLQ RPCFAVDTHI FRLCRWLGWI PVRANEVTAF SHLEVRIPDH
     LKYSLHQLFI RHGKTCPRCR AATGESSAGW EDGCVIDHLL TRDGKRKGNG PTVVPKKKAA
     AKSAAGKRKR MNKDSEEEET DESESSISNE TNDE
//
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