ID A0A0A2KSP1_PENEN Unreviewed; 272 AA.
AC A0A0A2KSP1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA polymerase epsilon subunit D {ECO:0000256|ARBA:ARBA00039775};
DE AltName: Full=DNA polymerase II subunit D {ECO:0000256|ARBA:ARBA00042096};
GN ORFNames=PEX2_100660 {ECO:0000313|EMBL:KGO60801.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO60801.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO60801.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO60801.1,
RC ECO:0000313|Proteomes:UP000030143};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KGO60801.1}.
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DR EMBL; JQFZ01000062; KGO60801.1; -; Genomic_DNA.
DR RefSeq; XP_016601811.1; XM_016747336.1.
DR AlphaFoldDB; A0A0A2KSP1; -.
DR STRING; 27334.A0A0A2KSP1; -.
DR GeneID; 27682756; -.
DR HOGENOM; CLU_043417_2_0_1; -.
DR OrthoDB; 1384627at2759; -.
DR PhylomeDB; A0A0A2KSP1; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR46172; DNA POLYMERASE EPSILON SUBUNIT 3; 1.
DR PANTHER; PTHR46172:SF1; DNA POLYMERASE EPSILON SUBUNIT 3; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 56..114
FT /note="Transcription factor CBF/NF-Y/archaeal histone"
FT /evidence="ECO:0000259|Pfam:PF00808"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 29754 MW; AA5F036D54F4B9D5 CRC64;
MPPRKSTSSV TPADPDDSLL QQSPPAPQTD KPIFATEQQL KARAEAGASV EDYLLPRSLT
IRLAKSVLPP NTTIQKDAVL AMQKAATVFV SYLSSHANDA TLKRTIAPSD VFNALSELEL
DSFRGRLEQE LEAYMEIKAG KRKPKKVDEN GSTQDALGEG PTQADGDIEM VDNPAKRVKR
DGDVEAPVGP PAGDDGDETQ EEDVEEEEED DESEDDEEEE EDRAPREDNL EHVEDLDREP
GARRGPYDPD AEETDEDEDG PGSQLRDDLG LG
//
