PCNA_CHATD
ID PCNA_CHATD Reviewed; 259 AA.
AC G0SF70;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Proliferating cell nuclear antigen;
DE Short=PCNA;
GN ORFNames=CTHT_0061010;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2]
RP GENE MODEL REVISION.
RA MacNeill S.;
RL Submitted (APR-2021) to UniProtKB.
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. Involved in DNA repair. {ECO:0000250|UniProtKB:P15873}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P15873}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15873}.
CC -!- PTM: Monoubiquitinated on Lys-164 upon DNA damage, and then
CC polyubiquitinated through 'Lys-63'-linkage.
CC {ECO:0000250|UniProtKB:P15873}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS18086.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL988046; EGS18086.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006696417.1; XM_006696354.1.
DR PDB; 7O1E; X-ray; 2.34 A; A=2-259.
DR PDB; 7O1F; X-ray; 2.45 A; A/B/C/D/E/F=2-259.
DR PDBsum; 7O1E; -.
DR PDBsum; 7O1F; -.
DR SMR; G0SF70; -.
DR STRING; 759272.G0SF70; -.
DR EnsemblFungi; EGS18086; EGS18086; CTHT_0061010.
DR GeneID; 18260139; -.
DR KEGG; cthr:CTHT_0061010; -.
DR eggNOG; KOG1636; Eukaryota.
DR HOGENOM; CLU_043978_3_0_1; -.
DR OrthoDB; 1012066at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR GO; GO:0043626; C:PCNA complex; IEA:EnsemblFungi.
DR GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006272; P:leading strand elongation; IEA:EnsemblFungi.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IEA:EnsemblFungi.
DR GO; GO:0000710; P:meiotic mismatch repair; IEA:EnsemblFungi.
DR GO; GO:1903459; P:mitotic DNA replication lagging strand elongation; IEA:EnsemblFungi.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:EnsemblFungi.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:EnsemblFungi.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IEA:EnsemblFungi.
DR GO; GO:1902394; P:positive regulation of exodeoxyribonuclease activity; IEA:EnsemblFungi.
DR GO; GO:1903022; P:positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands; IEA:EnsemblFungi.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0070914; P:UV-damage excision repair; IEA:EnsemblFungi.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
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 PANTHER; PTHR11352:SF0; PTHR11352:SF0; 1.
DR Pfam; PF02747; PCNA_C; 1.
DR Pfam; PF00705; PCNA_N; 1.
DR PRINTS; PR00339; PCNACYCLIN.
DR TIGRFAMs; TIGR00590; pcna; 1.
DR PROSITE; PS01251; PCNA_1; 1.
DR PROSITE; PS00293; PCNA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..259
FT /note="Proliferating cell nuclear antigen"
FT /id="PRO_0000453181"
FT DNA_BIND 61..80
FT /evidence="ECO:0000255"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15873"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15873"
SQ SEQUENCE 259 AA; 28588 MW; ACD98C1E223EA706 CRC64;
MLEARLEQAS ILKKVVDAIK DLVQDCNFDC NDSGIALQAM DNSHVALVSM MLKAEGFSPY
RCDRNIALGV NLTSLTKVLR AAQNEDILTL KAEDAPDVLN LVFESSETDR ISEYDLKLMD
IDQEHLGIPE TEYAATITMP SNEFKRITTD LMAMSESVTI EANKDGVKFS CQGDIGNGSV
TLRQHTNVEK PNESIEIELS EPVSLTFSLK YLVNFCKASA LSNTVKICLS NEVPLLVEYS
LGGSSYLRFY LAPKIGDDE
