ID   PCNA_NANEQ              Reviewed;         249 AA.
AC   Q74MV1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 89.
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=NEQ537;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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=AAR39379.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE017199; AAR39379.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q74MV1; -.
DR   SMR; Q74MV1; -.
DR   STRING; 228908.NEQ537; -.
DR   EnsemblBacteria; AAR39379; AAR39379; NEQ537.
DR   KEGG; neq:NEQ537; -.
DR   HOGENOM; CLU_043978_1_1_2; -.
DR   OMA; EMKLINM; -.
DR   Proteomes; UP000000578; 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; 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   TIGRFAMs; TIGR00590; pcna; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Reference proteome.
FT   CHAIN           1..249
FT                   /note="DNA polymerase sliding clamp"
FT                   /id="PRO_0000149201"
SQ   SEQUENCE   249 AA;  28115 MW;  ED862F8C38EDA7AF CRC64;
     MRVTFPDAKA LKKIVPIVAD LISEGQFVAT EEGIKLVAMD PASIAMVIWE MKPEAFIDYT
     IEGDKEIITV SMDDLKTIVK KLKQREMVVW ETDREKNKLK ILARGTIKKT FSIPLLEGEE
     TETPIPSLEY NNVVELDSKA IKEIIDDASA IADSLKFKAE PPSKLIIKAE GEMKEMTVEL
     TEGEDAVVSI DIQEEAYASY SIDYLKKFAK AADVSDIAIL KLKTDYPLWL EYRYLDKMTL
     IFILAPRSD