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Protein

DNA polymerase sliding clamp 3

Gene

pcn3

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. 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. Heterotrimer stimulates the Holliday junction resolvase Hjc.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:GCH2-391-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase sliding clamp 3UniRule annotation
Alternative name(s):
Proliferating cell nuclear antigen homolog 3UniRule annotation
Short name:
PCNA3UniRule annotation
Gene namesi
Name:pcn3UniRule annotation
Synonyms:pcnA-1
Ordered Locus Names:SSO0405
ORF Names:C41_016
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...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244DNA polymerase sliding clamp 3PRO_0000149214Add
BLAST

Interactioni

Subunit structurei

Does not individually interact with either of the other PCNA subunits, but is recruited to a PCNA1-PCNA2 heterodimer; does not form homotrimers (PubMed:12535540, PubMed:18703842). 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. This subunit interacts with DNA ligase, RfcL, XPF, and weakly with DNA polymerase I (PubMed:12535540).8 Publications

Protein-protein interaction databases

STRINGi273057.SSO0405.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi8 – 2114Combined sources
Beta strandi23 – 297Combined sources
Beta strandi31 – 399Combined sources
Beta strandi43 – 5210Combined sources
Helixi53 – 553Combined sources
Beta strandi57 – 604Combined sources
Beta strandi65 – 706Combined sources
Helixi71 – 788Combined sources
Beta strandi86 – 938Combined sources
Beta strandi96 – 11217Combined sources
Beta strandi129 – 1357Combined sources
Helixi136 – 14611Combined sources
Turni147 – 1493Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi172 – 1776Combined sources
Turni178 – 1803Combined sources
Beta strandi183 – 1908Combined sources
Beta strandi192 – 1976Combined sources
Helixi198 – 2036Combined sources
Helixi204 – 2107Combined sources
Beta strandi212 – 2198Combined sources
Beta strandi222 – 2298Combined sources
Helixi231 – 2333Combined sources
Beta strandi235 – 2406Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HIIX-ray2.79C/Z1-244[»]
2HIKX-ray3.30C/N/Z1-244[»]
2IJXX-ray1.90A/B/C/D1-244[»]
2IX2X-ray2.20C1-244[»]
2NTIX-ray2.50C/F/I1-244[»]
ProteinModelPortaliP57765.
SMRiP57765. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57765.

Family & Domainsi

Sequence similaritiesi

Belongs to the PCNA family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00488. Archaea.
COG0592. LUCA.
HOGENOMiHOG000222371.
InParanoidiP57765.
KOiK04802.
OMAiKCANSDD.

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.

P57765-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVVYDDVRV LKDIIQALAR LVDEAVLKFK QDSVELVALD RAHISLISVN
60 70 80 90 100
LPREMFKEYD VNDEFKFGFN TQYLMKILKV AKRKEAIEIA SESPDSVIIN
110 120 130 140 150
IIGSTNREFN VRNLEVSEQE IPEINLQFDI SATISSDGFK SAISEVSTVT
160 170 180 190 200
DNVVVEGHED RILIKAEGES EVEVEFSKDT GGLQDLEFSK ESKNSYSAEY
210 220 230 240
LDDVLSLTKL SDYVKISFGN QKPLQLFFNM EGGGKVTYLL APKV
Length:244
Mass (Da):27,459
Last modified:February 21, 2001 - v1
Checksum:i191C3C1267F1F5D1
GO

Sequence cautioni

The sequence AAK40734.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40734.1. Different initiation.
PIRiG90184.
RefSeqiWP_009988781.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK40734; AAK40734; SSO0405.
GeneIDi27426704.
KEGGisso:SSO0405.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40734.1. Different initiation.
PIRiG90184.
RefSeqiWP_009988781.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HIIX-ray2.79C/Z1-244[»]
2HIKX-ray3.30C/N/Z1-244[»]
2IJXX-ray1.90A/B/C/D1-244[»]
2IX2X-ray2.20C1-244[»]
2NTIX-ray2.50C/F/I1-244[»]
ProteinModelPortaliP57765.
SMRiP57765. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0405.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK40734; AAK40734; SSO0405.
GeneIDi27426704.
KEGGisso:SSO0405.

Phylogenomic databases

eggNOGiarCOG00488. Archaea.
COG0592. LUCA.
HOGENOMiHOG000222371.
InParanoidiP57765.
KOiK04802.
OMAiKCANSDD.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-391-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP57765.

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. "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 DPO1; LIG AND RFCL, 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, SUBUNIT.
  6. "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: SUBUNIT.
  7. "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: SUBUNIT.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), SUBUNIT.
  9. "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.
  10. "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 (1.90 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiPCNA3_SULSO
AccessioniPrimary (citable) accession number: P57765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: July 6, 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.