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Database: UniProt
Entry: A0A165MCE6_9APHY
LinkDB: A0A165MCE6_9APHY
Original site: A0A165MCE6_9APHY 
ID   A0A165MCE6_9APHY        Unreviewed;       362 AA.
AC   A0A165MCE6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Proliferating cell nuclear antigen {ECO:0000256|RuleBase:RU000641};
GN   ORFNames=DAEQUDRAFT_716397 {ECO:0000313|EMBL:KZT65497.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT65497.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT65497.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT65497.1,
RC   ECO:0000313|Proteomes:UP000076727};
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   -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase delta
CC       and is involved in the control of eukaryotic DNA replication by
CC       increasing the polymerase's processibility during elongation of the
CC       leading strand. {ECO:0000256|RuleBase:RU000641}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000641}.
CC   -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000256|ARBA:ARBA00010462,
CC       ECO:0000256|RuleBase:RU003671}.
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DR   EMBL; KV429104; KZT65497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165MCE6; -.
DR   STRING; 1314783.A0A165MCE6; -.
DR   OrthoDB; 118939at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   CDD; cd00577; PCNA; 1.
DR   Gene3D; 3.70.10.10; -; 1.
DR   Gene3D; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 1.
DR   HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR   InterPro; IPR046938; DNA_clamp_sf.
DR   InterPro; IPR000730; Pr_cel_nuc_antig.
DR   InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR   InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR   InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR   NCBIfam; TIGR00590; pcna; 1.
DR   PANTHER; PTHR11352; PROLIFERATING CELL NUCLEAR ANTIGEN; 1.
DR   PANTHER; PTHR11352:SF0; PROLIFERATING CELL NUCLEAR ANTIGEN; 1.
DR   Pfam; PF02747; PCNA_C; 2.
DR   Pfam; PF00705; PCNA_N; 1.
DR   PRINTS; PR00339; PCNACYCLIN.
DR   SUPFAM; SSF55979; DNA clamp; 2.
DR   PROSITE; PS01251; PCNA_1; 1.
DR   PROSITE; PS00293; PCNA_2; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|RuleBase:RU003671};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003671};
KW   Nucleus {ECO:0000256|RuleBase:RU000641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          1..124
FT                   /note="Proliferating cell nuclear antigen PCNA N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00705"
FT   DOMAIN          128..191
FT                   /note="Proliferating cell nuclear antigen PCNA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02747"
FT   DOMAIN          294..358
FT                   /note="Proliferating cell nuclear antigen PCNA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02747"
FT   REGION          180..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..213
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..267
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  40463 MW;  878A952D0FFB1429 CRC64;
     MLEARLNEAA TLKRLLDAIK ELVTDANFEC NEEGLTLQAM DNSHVALVAV KLKASGFKRY
     RCDRPIPLGV NIASFTKVLK CAKDDDVCIL KANDDADVLS LTYEARNTDR IAEYEMKLMD
     IDADTLNIPD TDYDARVTMP SSEFGRIVRD LSLLGESVRI EVSKEGVRFI SDGEAANGNV
     LLRDTQASTR KGGSSSKQED AEEEDEPEEE EEDEDKPTKK KIKKEKVKKE EGEGKGEEDV
     EMNGDGEEDD EQEFKPKGED DEEDEEEESS SKKRKKAPAK NAKPSKKAKK DDDDELPEGV
     KVEMNAHVNL TFSLKYLVNF SKSSSLSNVV QLMMSNDVPL LVSYEFGQGH IRYYLAPKIG
     DD
//
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