PCNA1_THEKO
ID PCNA1_THEKO Reviewed; 249 AA.
AC Q5JF32;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=DNA polymerase sliding clamp 1 {ECO:0000255|HAMAP-Rule:MF_00317};
DE AltName: Full=Proliferating cell nuclear antigen homolog 1 {ECO:0000255|HAMAP-Rule:MF_00317};
DE Short=PCNA 1 {ECO:0000255|HAMAP-Rule:MF_00317};
GN Name=pcn1 {ECO:0000255|HAMAP-Rule:MF_00317}; OrderedLocusNames=TK0535;
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).
RN [3] {ECO:0007744|PDB:5DA7, ECO:0007744|PDB:5DAI}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH TIP, ACTIVITY
RP REGULATION, SUBUNIT, AND INTERACTION WITH TIP.
RX PubMed=27141962; DOI=10.1093/nar/gkw351;
RA Altieri A.S., Ladner J.E., Li Z., Robinson H., Sallman Z.F., Marino J.P.,
RA Kelman Z.;
RT "A small protein inhibits proliferating cell nuclear antigen by breaking
RT the DNA clamp.";
RL Nucleic Acids Res. 44:6232-6241(2016).
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, ECO:0000269|PubMed:27141962}.
CC -!- SUBUNIT: Homotrimer (PubMed:27141962). The subunits circularize to form
CC a toroid; DNA passes through its center. Replication factor C (RFC) is
CC required to load the toroid on the DNA (By similarity). Interacts with
CC TIP (PubMed:24728986, PubMed:27141962). {ECO:0000255|HAMAP-
CC Rule:MF_00317, ECO:0000269|PubMed:24728986,
CC ECO:0000269|PubMed:27141962}.
CC -!- INTERACTION:
CC Q5JF32; Q5JF32: pcn1; NbExp=3; IntAct=EBI-15908613, EBI-15908613;
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
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DR EMBL; AP006878; BAD84724.1; -; Genomic_DNA.
DR RefSeq; WP_011249490.1; NC_006624.1.
DR PDB; 3LX1; X-ray; 2.00 A; A=1-249.
DR PDB; 5DA7; X-ray; 2.80 A; A/D=1-249.
DR PDB; 5DAI; X-ray; 2.00 A; A=1-249.
DR PDB; 6KNB; EM; 6.90 A; C/D/E=1-249.
DR PDB; 6KNC; EM; 9.30 A; C/D/E=1-249.
DR PDBsum; 3LX1; -.
DR PDBsum; 5DA7; -.
DR PDBsum; 5DAI; -.
DR PDBsum; 6KNB; -.
DR PDBsum; 6KNC; -.
DR AlphaFoldDB; Q5JF32; -.
DR SMR; Q5JF32; -.
DR DIP; DIP-59610N; -.
DR STRING; 69014.TK0535; -.
DR EnsemblBacteria; BAD84724; BAD84724; TK0535.
DR GeneID; 3234167; -.
DR KEGG; tko:TK0535; -.
DR PATRIC; fig|69014.16.peg.523; -.
DR eggNOG; arCOG00488; Archaea.
DR HOGENOM; CLU_043978_1_0_2; -.
DR InParanoid; Q5JF32; -.
DR OMA; TIRKDPN; -.
DR OrthoDB; 70433at2157; -.
DR PhylomeDB; Q5JF32; -.
DR EvolutionaryTrace; Q5JF32; -.
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 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 1"
FT /id="PRO_0000149208"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3LX1"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:3LX1"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3LX1"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 95..114
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3LX1"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:3LX1"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:3LX1"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3LX1"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:3LX1"
SQ SEQUENCE 249 AA; 28239 MW; AC836C2F0E2C79CB CRC64;
MPFEVVFDGA KEFADLIATA SNLIDEAAFK FTEEGISMRA MDPSRVVLID LNLPESIFSK
YEVEEPETIG INMDQFKKIL KRGKAKDTLI LRKGDENFLE ITFEGTAKRT FRLPLIDVEE
LELELPELPF TAKVVLLGEV LKEGIKDASL VSDAIKFIAK ENEFTMKAEG ETNEVEIRLT
LEDEGLLDLE VEEETKSAYG IRYLSDMVKG IGKADEVILR FGNEMPLQME YMIRDEGRLT
FLLAPRVEE
