PCNA_PYRFU
ID PCNA_PYRFU Reviewed; 249 AA.
AC O73947;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=DNA polymerase sliding clamp {ECO:0000255|HAMAP-Rule:MF_00317};
DE AltName: Full=Proliferating cell nuclear antigen homolog {ECO:0000255|HAMAP-Rule:MF_00317};
DE Short=PCNA {ECO:0000255|HAMAP-Rule:MF_00317};
GN Name=pcn {ECO:0000255|HAMAP-Rule:MF_00317}; OrderedLocusNames=PF0983;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10542158; DOI=10.1128/jb.181.21.6591-6599.1999;
RA Cann I.K.O., Ishino S., Hayashi I., Komori K., Toh H., Morikawa K.,
RA Ishino Y.;
RT "Functional interactions of a homolog of proliferating cell nuclear antigen
RT with DNA polymerases in Archaea.";
RL J. Bacteriol. 181:6591-6599(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP INTERACTION WITH HJC, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430863; DOI=10.1073/pnas.96.16.8873;
RA Komori K., Sakae S., Shinagawa H., Morikawa K., Ishino Y.;
RT "A Holliday junction resolvase from Pyrococcus furiosus: functional
RT similarity to Escherichia coli RuvC provides evidence for conserved
RT mechanism of homologous recombination in Bacteria, Eukarya, and Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8873-8878(1999).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11274122; DOI=10.1128/jb.183.8.2614-2623.2001;
RA Cann I.K.O., Ishino S., Yuasa M., Daiyasu H., Toh H., Ishino Y.;
RT "Biochemical analysis of replication factor C from the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 183:2614-2623(2001).
RN [5]
RP FUNCTION, INTERACTION WITH HEL308, AND SUBUNIT.
RX PubMed=16436047; DOI=10.1111/j.1365-2443.2006.00925.x;
RA Fujikane R., Shinagawa H., Ishino Y.;
RT "The archaeal Hjm helicase has recQ-like functions, and may be involved in
RT repair of stalled replication fork.";
RL Genes Cells 11:99-110(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF MET-73.
RX PubMed=11266590; DOI=10.1110/ps.36401;
RA Matsumiya S., Ishino Y., Morikawa K.;
RT "Crystal structure of an archaeal DNA sliding clamp: proliferating cell
RT nuclear antigen from Pyrococcus furiosus.";
RL Protein Sci. 10:17-23(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=12296822; DOI=10.1046/j.1365-2443.2002.00572.x;
RA Matsumiya S., Ishino S., Ishino Y., Morikawa K.;
RT "Physical interaction between proliferating cell nuclear antigen and
RT replication factor C from Pyrococcus furiosus.";
RL Genes Cells 7:911-922(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF ASP-143
RP AND 143-ASP--ASP-147.
RX PubMed=12649440; DOI=10.1110/ps.0234503;
RA Matsumiya S., Ishino S., Ishino Y., Morikawa K.;
RT "Intermolecular ion pairs maintain the toroidal structure of Pyrococcus
RT furiosus PCNA.";
RL Protein Sci. 12:823-831(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS).
RA Nishida H., Mayanagi K., Kiyonari S., Sato Y., Ishino Y., Morikawa K.;
RT "Structural determinant for switching between the polymerase and
RT exonuclease modes in the PCNA-replicative DNA polymerase complex.";
RL Submitted (NOV-2009) to the PDB data bank.
CC -!- FUNCTION: Sliding clamp subunit that acts as a moving platform for DNA
CC processing. Responsible for tethering the catalytic subunit of DNA
CC polymerase to DNA during high-speed replication. Unlike its eukaryotic
CC paralog, loads on circular DNA without the replication factor C (RFC)
CC clamp loader, although RFC greatly increases loading efficiency.
CC Stimulates the ATPase activity of replication factor C (RFC) in the
CC presence of ssDNA. Stimulates the helicase activity of Hel308 and may
CC alter its substrate specificity. {ECO:0000269|PubMed:11274122,
CC ECO:0000269|PubMed:12296822, ECO:0000269|PubMed:16436047}.
CC -!- SUBUNIT: Homotrimer which circularizes head-to-tail (head is a N-
CC terminus, tail is at C-terminus) to form a toroid. RFC opens the toroid
CC so it can load on DNA. Interacts with both Pol I (pol) and Pol II
CC (polB-polC), with Hel308 (hjm) and with Hjc. Interaction with the C-
CC terminal PIP-box of RfcL may stabilize the toroidal structure.
CC {ECO:0000269|PubMed:10430863, ECO:0000269|PubMed:11266590,
CC ECO:0000269|PubMed:12296822, ECO:0000269|PubMed:12649440,
CC ECO:0000269|PubMed:16436047}.
CC -!- INTERACTION:
CC O73947; P81412: polB; NbExp=2; IntAct=EBI-15762053, EBI-15906191;
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
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DR EMBL; AB017486; BAA33020.2; -; Genomic_DNA.
DR EMBL; AE009950; AAL81107.1; -; Genomic_DNA.
DR RefSeq; WP_011012120.1; NC_018092.1.
DR PDB; 1GE8; X-ray; 2.10 A; A=1-249.
DR PDB; 1ISQ; X-ray; 2.30 A; A=1-249.
DR PDB; 1IZ4; X-ray; 2.00 A; A=1-249.
DR PDB; 1IZ5; X-ray; 1.80 A; A/B=1-249.
DR PDB; 3A2F; X-ray; 2.67 A; B=2-249.
DR PDB; 5AUJ; X-ray; 2.50 A; A=1-249.
DR PDBsum; 1GE8; -.
DR PDBsum; 1ISQ; -.
DR PDBsum; 1IZ4; -.
DR PDBsum; 1IZ5; -.
DR PDBsum; 3A2F; -.
DR PDBsum; 5AUJ; -.
DR AlphaFoldDB; O73947; -.
DR SMR; O73947; -.
DR DIP; DIP-48777N; -.
DR IntAct; O73947; 2.
DR STRING; 186497.PF0983; -.
DR PRIDE; O73947; -.
DR EnsemblBacteria; AAL81107; AAL81107; PF0983.
DR GeneID; 41712796; -.
DR KEGG; pfu:PF0983; -.
DR PATRIC; fig|186497.12.peg.1042; -.
DR eggNOG; arCOG00488; Archaea.
DR HOGENOM; CLU_043978_1_0_2; -.
DR OMA; EMKLINM; -.
DR OrthoDB; 70433at2157; -.
DR PhylomeDB; O73947; -.
DR EvolutionaryTrace; O73947; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR IDEAL; IID90015; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Reference proteome.
FT CHAIN 1..249
FT /note="DNA polymerase sliding clamp"
FT /id="PRO_0000149206"
FT MUTAGEN 73
FT /note="M->L: No observable effect."
FT /evidence="ECO:0000269|PubMed:11266590"
FT MUTAGEN 143..147
FT /note="DAVKD->AAVKA: No homotrimer formation. Stimulates
FT ATPase activity of RFC, no stimulation of DNA synthesis by
FT Pol I in presence and absence of RFC. Crystallizes as tail-
FT to-tail homodimers."
FT /evidence="ECO:0000269|PubMed:12649440"
FT MUTAGEN 143
FT /note="D->A: Small amount of homotrimer in solution.
FT Stimulates ATPase activity of RFC and DNA synthesis by Pol
FT I in presence and absence of RFC. Crystallizes as tail-to-
FT tail homodimers."
FT /evidence="ECO:0000269|PubMed:12649440"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1IZ5"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:1IZ5"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1IZ5"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 95..114
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1IZ5"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:1IZ5"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1IZ4"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1IZ5"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1IZ5"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:1IZ5"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1IZ5"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:1IZ5"
SQ SEQUENCE 249 AA; 28005 MW; B6932127B001FA74 CRC64;
MPFEIVFEGA KEFAQLIDTA SKLIDEAAFK VTEDGISMRA MDPSRVVLID LNLPSSIFSK
YEVVEPETIG VNMDHLKKIL KRGKAKDTLI LKKGEENFLE ITIQGTATRT FRVPLIDVEE
MEVDLPELPF TAKVVVLGEV LKDAVKDASL VSDSIKFIAR ENEFIMKAEG ETQEVEIKLT
LEDEGLLDIE VQEETKSAYG VSYLSDMVKG LGKADEVTIK FGNEMPMQME YYIRDEGRLT
FLLAPRVEE
