ID   PCNA_NITMS              Reviewed;         248 AA.
AC   A9A2X4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Nmar_1755;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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}.
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DR   EMBL; CP000866; ABX13651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A2X4; -.
DR   SMR; A9A2X4; -.
DR   STRING; 436308.Nmar_1755; -.
DR   EnsemblBacteria; ABX13651; ABX13651; Nmar_1755.
DR   KEGG; nmr:Nmar_1755; -.
DR   eggNOG; arCOG00488; Archaea.
DR   HOGENOM; CLU_043978_3_0_2; -.
DR   OMA; EMKLINM; -.
DR   PhylomeDB; A9A2X4; -.
DR   Proteomes; UP000000792; 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: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; 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.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Reference proteome.
FT   CHAIN           1..248
FT                   /note="DNA polymerase sliding clamp"
FT                   /id="PRO_1000115816"
SQ   SEQUENCE   248 AA;  27175 MW;  5822C2A226B2A5D6 CRC64;
     MTFGAKTSGS DDLKAIISAI STLVEEATFV ATAEGISFRG MDPSHVALID ISWPNSAFEK
     YECDSDIKFG VRIDEFSKLI KRADKKDSIE ISISEQNMLL VTVGKNKKYK MRLIESSATD
     TPLPKIPYDS KIILSSSKFD KILGDVQVVS DYLTIHTSDS KGDFSGKGDS GEVVIDLDKD
     DEGIEEISSK EDSVGTYSLE YLNPVVKAVG TTAGFITCEF SSAKPLRIEF KVANIGRIHF
     YLAPRVES