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Protein

DNA polymerase sliding clamp

Gene

pcn

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Unlike its eukaryotic paralog, loads on circular DNA without the replication factor C (RFC) clamp loader, although RFC greatly increases loading efficiency. Stimulates the ATPase activity of replication factor C (RFC) in the presence of ssDNA. Stimulates the helicase activity of Hel308 and may alter its substrate specificity.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase sliding clampUniRule annotation
Alternative name(s):
Proliferating cell nuclear antigen homologUniRule annotation
Short name:
PCNAUniRule annotation
Gene namesi
Name:pcnUniRule annotation
Ordered Locus Names:PF0983
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731M → L: No observable effect. 1 Publication
Mutagenesisi143 – 1475DAVKD → AAVKA: No homotrimer formation. Stimulates ATPase activity of RFC, no stimulation of DNA synthesis by Pol I in presence and absence of RFC. Crystallizes as tail-to-tail homodimers. 1 Publication
Mutagenesisi143 – 1431D → A: Small amount of homotrimer in solution. Stimulates ATPase activity of RFC and DNA synthesis by Pol I in presence and absence of RFC. Crystallizes as tail-to-tail homodimers. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249DNA polymerase sliding clampPRO_0000149206Add
BLAST

Proteomic databases

PRIDEiO73947.

Interactioni

Subunit structurei

Homotrimer which circularizes head-to-tail (head is a N-terminus, tail is at C-terminus) to form a toroid. RFC opens the toroid so it can load on DNA. Interacts with both Pol I (pol) and Pol II (polB-polC), with Hel308 (hjm) and with Hjc. Interaction with the C-terminal PIP-box of RfcL may stabilize the toroidal structure.5 Publications

Protein-protein interaction databases

DIPiDIP-48777N.
STRINGi186497.PF0983.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi10 – 2011Combined sources
Beta strandi25 – 317Combined sources
Beta strandi33 – 419Combined sources
Beta strandi45 – 5410Combined sources
Helixi55 – 573Combined sources
Beta strandi58 – 658Combined sources
Beta strandi67 – 726Combined sources
Helixi73 – 808Combined sources
Beta strandi88 – 936Combined sources
Beta strandi95 – 11420Combined sources
Beta strandi132 – 1376Combined sources
Helixi138 – 14811Combined sources
Turni149 – 1513Combined sources
Beta strandi153 – 1608Combined sources
Beta strandi163 – 1697Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi174 – 1807Combined sources
Turni181 – 1844Combined sources
Beta strandi185 – 1939Combined sources
Beta strandi195 – 2006Combined sources
Helixi201 – 2088Combined sources
Beta strandi216 – 2216Combined sources
Beta strandi227 – 2337Combined sources
Turni234 – 2363Combined sources
Beta strandi237 – 2437Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GE8X-ray2.10A1-249[»]
1ISQX-ray2.30A1-249[»]
1IZ4X-ray2.00A1-249[»]
1IZ5X-ray1.80A/B1-249[»]
3A2FX-ray2.67B2-249[»]
ProteinModelPortaliO73947.
SMRiO73947. Positions 2-247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO73947.

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00488. Archaea.
COG0592. LUCA.
HOGENOMiHOG000222371.
KOiK04802.
OMAiDIFYMEA.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch.
InterProiIPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERiPTHR11352. PTHR11352. 1 hit.
PfamiPF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]
PRINTSiPR00339. PCNACYCLIN.
TIGRFAMsiTIGR00590. pcna. 1 hit.
PROSITEiPS01251. PCNA_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O73947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFEIVFEGA KEFAQLIDTA SKLIDEAAFK VTEDGISMRA MDPSRVVLID
60 70 80 90 100
LNLPSSIFSK YEVVEPETIG VNMDHLKKIL KRGKAKDTLI LKKGEENFLE
110 120 130 140 150
ITIQGTATRT FRVPLIDVEE MEVDLPELPF TAKVVVLGEV LKDAVKDASL
160 170 180 190 200
VSDSIKFIAR ENEFIMKAEG ETQEVEIKLT LEDEGLLDIE VQEETKSAYG
210 220 230 240
VSYLSDMVKG LGKADEVTIK FGNEMPMQME YYIRDEGRLT FLLAPRVEE
Length:249
Mass (Da):28,005
Last modified:February 21, 2001 - v2
Checksum:iB6932127B001FA74
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017486 Genomic DNA. Translation: BAA33020.2.
AE009950 Genomic DNA. Translation: AAL81107.1.
RefSeqiWP_011012120.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81107; AAL81107; PF0983.
GeneIDi1468848.
KEGGipfu:PF0983.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017486 Genomic DNA. Translation: BAA33020.2.
AE009950 Genomic DNA. Translation: AAL81107.1.
RefSeqiWP_011012120.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GE8X-ray2.10A1-249[»]
1ISQX-ray2.30A1-249[»]
1IZ4X-ray2.00A1-249[»]
1IZ5X-ray1.80A/B1-249[»]
3A2FX-ray2.67B2-249[»]
ProteinModelPortaliO73947.
SMRiO73947. Positions 2-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48777N.
STRINGi186497.PF0983.

Proteomic databases

PRIDEiO73947.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81107; AAL81107; PF0983.
GeneIDi1468848.
KEGGipfu:PF0983.

Phylogenomic databases

eggNOGiarCOG00488. Archaea.
COG0592. LUCA.
HOGENOMiHOG000222371.
KOiK04802.
OMAiDIFYMEA.

Miscellaneous databases

EvolutionaryTraceiO73947.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch.
InterProiIPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERiPTHR11352. PTHR11352. 1 hit.
PfamiPF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]
PRINTSiPR00339. PCNACYCLIN.
TIGRFAMsiTIGR00590. pcna. 1 hit.
PROSITEiPS01251. PCNA_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in Archaea."
    Cann I.K.O., Ishino S., Hayashi I., Komori K., Toh H., Morikawa K., Ishino Y.
    J. Bacteriol. 181:6591-6599(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  3. "A Holliday junction resolvase from Pyrococcus furiosus: functional similarity to Escherichia coli RuvC provides evidence for conserved mechanism of homologous recombination in Bacteria, Eukarya, and Archaea."
    Komori K., Sakae S., Shinagawa H., Morikawa K., Ishino Y.
    Proc. Natl. Acad. Sci. U.S.A. 96:8873-8878(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HJC, SUBUNIT.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  4. "Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus."
    Cann I.K.O., Ishino S., Yuasa M., Daiyasu H., Toh H., Ishino Y.
    J. Bacteriol. 183:2614-2623(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  5. "The archaeal Hjm helicase has recQ-like functions, and may be involved in repair of stalled replication fork."
    Fujikane R., Shinagawa H., Ishino Y.
    Genes Cells 11:99-110(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HEL308, SUBUNIT.
  6. "Crystal structure of an archaeal DNA sliding clamp: proliferating cell nuclear antigen from Pyrococcus furiosus."
    Matsumiya S., Ishino Y., Morikawa K.
    Protein Sci. 10:17-23(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, MUTAGENESIS OF MET-73.
  7. "Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus."
    Matsumiya S., Ishino S., Ishino Y., Morikawa K.
    Genes Cells 7:911-922(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, SUBUNIT.
  8. "Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA."
    Matsumiya S., Ishino S., Ishino Y., Morikawa K.
    Protein Sci. 12:823-831(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, MUTAGENESIS OF ASP-143 AND 143-ASP--ASP-147.
  9. "Structural determinant for switching between the polymerase and exonuclease modes in the PCNA-replicative DNA polymerase complex."
    Nishida H., Mayanagi K., Kiyonari S., Sato Y., Ishino Y., Morikawa K.
    Submitted (NOV-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS).

Entry informationi

Entry nameiPCNA_PYRFU
AccessioniPrimary (citable) accession number: O73947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 21, 2001
Last modified: November 11, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.