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Protein

DNA polymerase sliding clamp 1

Gene

pcn1

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

One of the sliding clamp subunits that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Heterotrimer stimulates the Holliday junction resolvase Hjc. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-383-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase sliding clamp 1UniRule annotation
Alternative name(s):
Proliferating cell nuclear antigen homolog 1UniRule annotation
Short name:
PCNA1UniRule annotation
Gene namesi
Name:pcn1UniRule annotation
Synonyms:pcnA-like
Ordered Locus Names:SSO0397
ORF Names:C41_008
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1163YIK → ELE: Loss of interaction with PCNA3, no change with PCNA2. 1 Publication
Mutagenesisi175 – 1773KRY → EED: Loss of interaction with both PCNA3 and PCNA2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249DNA polymerase sliding clamp 1PRO_0000149215Add
BLAST

Interactioni

Subunit structurei

Forms heterodimers with PCNA2, which then recruit PCNA3; does not form homotrimers (PubMed:12535540, PubMed:18703842). The heterodimers interact with RfcS homotetramers (PubMed:12535540). Heterotrimer which circularizes head-to-tail (head is at N-terminus, tail is at C-terminus) to form a toroid; DNA passes through its center. Replication factor C (RFC) is required to load the toroid on the DNA. Heterotrimer interacts, probably via this subunit, with flap endonuclease 1 (fen) (PubMed:12535540), Hjc (PubMed:17011573), Dpo4 (PubMed:19054331), and XPF (PubMed:12675797).8 Publications

Protein-protein interaction databases

DIPiDIP-48854N.
STRINGi273057.SSO0397.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi9 – 1911Combined sources
Turni20 – 223Combined sources
Beta strandi24 – 307Combined sources
Beta strandi32 – 409Combined sources
Beta strandi44 – 5310Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 615Combined sources
Beta strandi66 – 705Combined sources
Helixi72 – 798Combined sources
Beta strandi87 – 937Combined sources
Beta strandi95 – 10410Combined sources
Turni105 – 1073Combined sources
Beta strandi110 – 1167Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi134 – 1385Combined sources
Helixi140 – 15314Combined sources
Beta strandi155 – 1628Combined sources
Beta strandi165 – 1728Combined sources
Beta strandi175 – 1839Combined sources
Beta strandi185 – 19410Combined sources
Beta strandi197 – 2015Combined sources
Helixi202 – 2109Combined sources
Turni211 – 2144Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi240 – 2456Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HIIX-ray2.79A/X1-249[»]
2HIKX-ray3.30A/L/X1-249[»]
2IO4X-ray2.60A/C1-249[»]
2IX2X-ray2.20A1-249[»]
2IZOX-ray2.90C1-249[»]
2NTIX-ray2.50A/D/G1-249[»]
3FDSX-ray2.05C1-249[»]
ProteinModelPortaliP57766.
SMRiP57766. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57766.

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00488. Archaea.
COG0592. LUCA.
HOGENOMiHOG000270356.
InParanoidiP57766.
KOiK04802.
OMAiKRGTRND.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch.
InterProiIPR000730. Pr_cel_nuc_antig.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERiPTHR11352. PTHR11352. 1 hit.
PfamiPF00705. PCNA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P57766-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKIVYPNAK DFFSFINSIT NVTDSIILNF TEDGIFSRHL TEDKVLMAIM
60 70 80 90 100
RIPKDVLSEY SIDSPTSVKL DVSSVKKILS KASSKKATIE LTETDSGLKI
110 120 130 140 150
IIRDEKSGAK STIYIKAEKG QVEQLTEPKV NLAVNFTTDE SVLNVIAADV
160 170 180 190 200
TLVGEEMRIS TEEDKIKIEA GEEGKRYVAF LMKDKPLKEL SIDTSASSSY
210 220 230 240
SAEMFKDAVK GLRGFSAPTM VSFGENLPMK IDVEAVSGGH MIFWIAPRL
Length:249
Mass (Da):27,536
Last modified:February 21, 2001 - v1
Checksum:i137EB10BE2C03F77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40726.1.
PIRiG90183.
RefSeqiWP_009988793.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK40726; AAK40726; SSO0397.
GeneIDi25403870.
KEGGisso:SSO0397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40726.1.
PIRiG90183.
RefSeqiWP_009988793.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HIIX-ray2.79A/X1-249[»]
2HIKX-ray3.30A/L/X1-249[»]
2IO4X-ray2.60A/C1-249[»]
2IX2X-ray2.20A1-249[»]
2IZOX-ray2.90C1-249[»]
2NTIX-ray2.50A/D/G1-249[»]
3FDSX-ray2.05C1-249[»]
ProteinModelPortaliP57766.
SMRiP57766. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48854N.
STRINGi273057.SSO0397.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK40726; AAK40726; SSO0397.
GeneIDi25403870.
KEGGisso:SSO0397.

Phylogenomic databases

eggNOGiarCOG00488. Archaea.
COG0592. LUCA.
HOGENOMiHOG000270356.
InParanoidiP57766.
KOiK04802.
OMAiKRGTRND.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-383-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP57766.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch.
InterProiIPR000730. Pr_cel_nuc_antig.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERiPTHR11352. PTHR11352. 1 hit.
PfamiPF00705. PCNA_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two DNA polymerase sliding clamps from the thermophilic archaeon Sulfolobus solfataricus."
    De Felice M., Sensen C.W., Charlebois R.L., Rossi M., Pisani F.M.
    J. Mol. Biol. 291:47-57(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus."
    Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D.
    Mol. Cell 11:275-282(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FEN AND PCNA2, SUBUNIT.
  4. "An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA."
    Roberts J.A., Bell S.D., White M.F.
    Mol. Microbiol. 48:361-371(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XPF, SUBUNIT.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  5. "PCNA activates the Holliday junction endonuclease Hjc."
    Dorazi R., Parker J.L., White M.F.
    J. Mol. Biol. 364:243-247(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HJC, SUBUNIT.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), SUBUNIT.
  7. "A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA."
    Pascal J.M., Tsodikov O.V., Hura G.L., Song W., Cotner E.A., Classen S., Tomkinson A.E., Tainer J.A., Ellenberger T.
    Mol. Cell 24:279-291(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS), SUBUNIT.
  8. "Structure of an archaeal PCNA1-PCNA2-FEN1 complex: elucidating PCNA subunit and client enzyme specificity."
    Dore A.S., Kilkenny M.L., Jones S.A., Oliver A.W., Roe S.M., Bell S.D., Pearl L.H.
    Nucleic Acids Res. 34:4515-4526(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PCNA2 AND FEN, SUBUNIT, MUTAGENESIS OF 114-TYR--LYS-116 AND 175-LYS--TYR-177.
  9. "Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening."
    Hlinkova V., Xing G., Bauer J., Shin Y.J., Dionne I., Rajashankar K.R., Bell S.D., Ling H.
    Acta Crystallogr. D 64:941-949(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-249, SUBUNIT.
  10. "Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA."
    Xing G., Kirouac K., Shin Y.J., Bell S.D., Ling H.
    Mol. Microbiol. 71:678-691(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 3-249 IN COMPLEX WITH DPO4, INTERACTION WITH DPO4, SUBUNIT.

Entry informationi

Entry nameiPCNA1_SULSO
AccessioniPrimary (citable) accession number: P57766
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: February 17, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.