ID   PCNA_THEVO              Reviewed;         246 AA.
AC   Q979S2;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=DNA polymerase sliding clamp {ECO:0000255|HAMAP-Rule:MF_00317};
DE   AltName: Full=Proliferating cell nuclear antigen homolog {ECO:0000255|HAMAP-Rule:MF_00317};
DE            Short=PCNA {ECO:0000255|HAMAP-Rule:MF_00317};
GN   Name=pcn {ECO:0000255|HAMAP-Rule:MF_00317}; OrderedLocusNames=TV1088;
GN   ORFNames=TVG1118724;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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   -!- 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. {ECO:0000255|HAMAP-Rule:MF_00317}.
CC   -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00317}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB60230.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000011; BAB60230.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q979S2; -.
DR   SMR; Q979S2; -.
DR   STRING; 273116.14325326; -.
DR   PRIDE; Q979S2; -.
DR   DNASU; 1441202; -.
DR   EnsemblBacteria; BAB60230; BAB60230; BAB60230.
DR   KEGG; tvo:TVG1118724; -.
DR   eggNOG; arCOG00488; Archaea.
DR   HOGENOM; CLU_043978_1_1_2; -.
DR   OMA; EMKLINM; -.
DR   PhylomeDB; Q979S2; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   DNA replication; DNA-binding.
FT   CHAIN           1..246
FT                   /note="DNA polymerase sliding clamp"
FT                   /id="PRO_0000149222"
SQ   SEQUENCE   246 AA;  27558 MW;  2AC0DAAB0B27A805 CRC64;
     MIRMNISVRN LKEITDLLST IVSEAKFKVD ENGMSVTAVD PAHVAMIRLE VPKEVFSEFR
     SDGTEEIALD IDRLKSVIRL ANSSENVGIT KDKEKLKFDL GNISKSVSLL DPSTIVTPKI
     PNIASEYYAI IKRSDFERGL RAAEDISDSI RFVLSSEGFR ATSHSESEES EMVLPKDMLS
     DLSCSDTIKS SYPLEYLLKF IKAVSSADSL KISFRDDYPL SIEFYLDQNP SAKIKGLFLL
     APRMEQ