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Database: UniProt
Entry: A0A165HV14_EXIGL
LinkDB: A0A165HV14_EXIGL
Original site: A0A165HV14_EXIGL 
ID   A0A165HV14_EXIGL        Unreviewed;       275 AA.
AC   A0A165HV14;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=EXIGLDRAFT_749641 {ECO:0000313|EMBL:KZV92500.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV92500.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV92500.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV92500.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KV426007; KZV92500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165HV14; -.
DR   STRING; 1314781.A0A165HV14; -.
DR   InParanoid; A0A165HV14; -.
DR   OrthoDB; 1384627at2759; -.
DR   Proteomes; UP000077266; 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:UP000077266}.
FT   DOMAIN          27..91
FT                   /note="Transcription factor CBF/NF-Y/archaeal histone"
FT                   /evidence="ECO:0000259|Pfam:PF00808"
FT   REGION          114..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..254
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   275 AA;  29820 MW;  A4FC87DBDB0777F1 CRC64;
     MPRKESAPTA KSQQDAVMGT EGIENYELPK SLVTKIAKSV IPENAKLQKD VVLALTKGST
     VFINYLTATA QDVATQRSHK TISAADVLKA LEIIEFGDMI PGVEKDLEAY RALQKSAPKA
     PRKSTGAAAK DKDKAAAPES TPKGKDKGKG KEKESEKDKD KEKEKEPAAT TTPGSRSSAR
     TRAKKQAAAA EEPAPAPAPA PAPTEDVTMA EEEEEDEEIA KFDEEDELEE EEEEEEEEEE
     EQDVPAEENG MDVDDENVAL AGQDFDKETS SRDDD
//
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