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Database: UniProt
Entry: A0A1V6Q5T6_9EURO
LinkDB: A0A1V6Q5T6_9EURO
Original site: A0A1V6Q5T6_9EURO 
ID   A0A1V6Q5T6_9EURO        Unreviewed;       844 AA.
AC   A0A1V6Q5T6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Proliferating cell nuclear antigen {ECO:0000256|RuleBase:RU000641};
GN   ORFNames=PENANT_c013G05403 {ECO:0000313|EMBL:OQD84242.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD84242.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
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:OQD84242.1}.
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DR   EMBL; MDYN01000013; OQD84242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6Q5T6; -.
DR   STRING; 416450.A0A1V6Q5T6; -.
DR   OrthoDB; 118939at2759; -.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0017022; F:myosin binding; 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; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 2.
DR   HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR   InterPro; IPR046938; DNA_clamp_sf.
DR   InterPro; IPR026859; Myosin-bd.
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:SF3; MYOSIN-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11352; PROLIFERATING CELL NUCLEAR ANTIGEN; 1.
DR   Pfam; PF02747; PCNA_C; 1.
DR   Pfam; PF00705; PCNA_N; 1.
DR   Pfam; PF12632; Vezatin; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|RuleBase:RU000641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        140..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          153..433
FT                   /note="Myosin-binding"
FT                   /evidence="ECO:0000259|Pfam:PF12632"
FT   DOMAIN          591..709
FT                   /note="Proliferating cell nuclear antigen PCNA N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00705"
FT   DOMAIN          714..839
FT                   /note="Proliferating cell nuclear antigen PCNA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02747"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  93062 MW;  5C16F89BABF9380E CRC64;
     MESLVYENSP LAEYLEGEGG HQESWPVEEN QSDDDHTSAF DFAPRGASKF QTRVRNKLPK
     PLDLRGTPQG EFAGKLYDAC SSALNVRLPR SDNERFLEQF GYVIVASQLL NEHSAPSYTS
     ASDVLSATQP TALPSLSTTF GIQGAIVTAC TSFSIAWLLH WSRSRTGSGL NPKKVGVLLI
     LVPVLGVLFY AFAKRQWLKY LRHQAVDAAG TFIGNAQGFD SAASASVVFI QEVELVSRGY
     RISTPLPPIS RLEDQIQTRR CLRLRRTVSE CFYSMLERYV RSENTLRPLT DEANLAKYYD
     IYDIGLEELA AIESSLSQRA NDDQYSLRAL RDLFGKLYSV RKSVLCCLLA LSADGGGSDI
     GRWSSAVEEM RELAAVTGDS MLKMTAILNE EDRDNIPPSP LPSASVSPSK DYLRAQIRRF
     SSLSQGVRAL HAKMHIVSEE SHASLERPDS ADYEAALLTQ YDSVGGDLRA LLQEWEAGKA
     ALVNQDRLSV DRSRPPSTLL MPMSPTPSLG GSTAVEGSPT DALKALNGEG RPDLTQTYDD
     EEIFEAVVLP ASRNKRVSLT RDERLARVRE DRARQATARE KVDANTNMLK ELEMASLLKR
     VVDAIKDLVQ DCNFDCNDSG IALQAMDNSH VALVSMLLRA EGFSPYRCDR NIALGINLLS
     LTKVLRAAQN EDILTLKAED SPDAVNLMFE SAETDRLSEY DIKLMDIDQE HLAIPETEYA
     ATVEMPSAEF QRICRDLNAL SESVVIEASK EGVKFSCQGD IGNGSVTIRQ HTNVDKPDQN
     VAISLSEPVA LTFSLKYLVN FCKASNLSSS VILHLSQEVP LLVEYGLGSG HLRFYLAPKI
     GDEE
//
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