PCNA2_THEKO
ID PCNA2_THEKO Reviewed; 253 AA.
AC Q5JFD3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=DNA polymerase sliding clamp 2 {ECO:0000255|HAMAP-Rule:MF_00317};
DE AltName: Full=Proliferating cell nuclear antigen homolog 2 {ECO:0000255|HAMAP-Rule:MF_00317};
DE Short=PCNA 2 {ECO:0000255|HAMAP-Rule:MF_00317};
GN Name=pcn2 {ECO:0000255|HAMAP-Rule:MF_00317}; OrderedLocusNames=TK0582;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP ACTIVITY REGULATION, AND INTERACTION WITH TIP.
RX PubMed=24728986; DOI=10.1093/nar/gku239;
RA Li Z., Huang R.Y., Yopp D.C., Hileman T.H., Santangelo T.J., Hurwitz J.,
RA Hudgens J.W., Kelman Z.;
RT "A novel mechanism for regulating the activity of proliferating cell
RT nuclear antigen by a small protein.";
RL Nucleic Acids Res. 42:5776-5789(2014).
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 and other proteins to DNA during high-speed replication.
CC {ECO:0000255|HAMAP-Rule:MF_00317}.
CC -!- ACTIVITY REGULATION: Inhibited by interaction with the PCNA inhibitor
CC TIP. {ECO:0000269|PubMed:24728986}.
CC -!- SUBUNIT: Homotrimer. The subunits circularize to form a toroid; DNA
CC passes through its center. Replication factor C (RFC) is required to
CC load the toroid on the DNA (By similarity). Interacts with TIP
CC (PubMed:24728986). {ECO:0000255|HAMAP-Rule:MF_00317,
CC ECO:0000269|PubMed:24728986}.
CC -!- INTERACTION:
CC Q5JFD3; Q5JFD3: pcn2; NbExp=3; IntAct=EBI-15908562, EBI-15908562;
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
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DR EMBL; AP006878; BAD84771.1; -; Genomic_DNA.
DR RefSeq; WP_011249537.1; NC_006624.1.
DR PDB; 3LX2; X-ray; 2.40 A; A/B/C=1-253.
DR PDBsum; 3LX2; -.
DR AlphaFoldDB; Q5JFD3; -.
DR SMR; Q5JFD3; -.
DR DIP; DIP-59609N; -.
DR STRING; 69014.TK0582; -.
DR EnsemblBacteria; BAD84771; BAD84771; TK0582.
DR GeneID; 3235115; -.
DR KEGG; tko:TK0582; -.
DR PATRIC; fig|69014.16.peg.567; -.
DR eggNOG; arCOG00488; Archaea.
DR HOGENOM; CLU_043978_1_1_2; -.
DR InParanoid; Q5JFD3; -.
DR OMA; EMKLINM; -.
DR OrthoDB; 70433at2157; -.
DR PhylomeDB; Q5JFD3; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
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 PROSITE; PS01251; PCNA_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Reference proteome.
FT CHAIN 1..253
FT /note="DNA polymerase sliding clamp 2"
FT /id="PRO_0000149209"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3LX2"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:3LX2"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3LX2"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 95..114
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3LX2"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:3LX2"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:3LX2"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3LX2"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:3LX2"
SQ SEQUENCE 253 AA; 28447 MW; 2460EF12BE490CAC CRC64;
MTFEIVFDSA REFESLIATL EKFFDEAVFQ VNMEGIQMRA IDPSRVVLVD LNLPEMLFSK
YSVESEEAIA FDLKRFLKVL KLARSRDTLV LRKGGENFLE VGLLGDENTW FKLPLIDANT
PEIEIPSLPW TVKAVVLAGA LKRAVKAAKL VSDSIYFMAT PEKLTFKAEG NDSEVRTVLT
MEDPGLLDLE HKMTKAKSAY GVAYLEDILR SLADADEVII RFGFDIPLLL KYMVRDAGEV
SFLIAPRVEE GRS
