ID PCNA3_SULTO Reviewed; 246 AA.
AC Q973F5; F9VNC0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=DNA polymerase sliding clamp 3 {ECO:0000255|HAMAP-Rule:MF_00317};
DE AltName: Full=Proliferating cell nuclear antigen homolog 3 {ECO:0000255|HAMAP-Rule:MF_00317};
DE Short=PCNA3 {ECO:0000255|HAMAP-Rule:MF_00317};
GN Name=pcn3 {ECO:0000255|HAMAP-Rule:MF_00317}; Synonyms=pcnC;
GN OrderedLocusNames=STK_09440;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION, INTERACTION WITH PCNA1 AND PCNA2, AND SUBUNIT.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=18782564; DOI=10.1016/j.bbrc.2008.08.150;
RA Lu S., Li Z., Wang Z., Ma X., Sheng D., Ni J., Shen Y.;
RT "Spatial subunit distribution and in vitro functions of the novel trimeric
RT PCNA complex from Sulfolobus tokodaii.";
RL Biochem. Biophys. Res. Commun. 376:369-374(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=21352919; DOI=10.1016/j.jsb.2011.02.006;
RA Kawai A., Hashimoto H., Higuchi S., Tsunoda M., Sato M., Nakamura K.T.,
RA Miyamoto S.;
RT "A novel heterotetrameric structure of the crenarchaeal PCNA2-PCNA3
RT complex.";
RL J. Struct. Biol. 174:443-450(2011).
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 (By
CC similarity). Both trimeric complexes inhibit DNA ligase and both 3'-5'
CC and 5'-3' activity of Hel308 (Hjm) helicase, but stimulate Hjc, the
CC Holliday junction cleavage enzyme. {ECO:0000255|HAMAP-Rule:MF_00317,
CC ECO:0000269|PubMed:18782564}.
CC -!- SUBUNIT: The subunits circularize to form a toroid; DNA passes through
CC its center. Replication factor C (RFC) is required to load the toroid
CC on the DNA (By similarity). Forms dimeric complexes with PCNA1 and
CC PCNA2, and trimeric complexes with PCNA123 and PCNA323; does not form
CC homotrimers (PubMed:18782564). Crystal structures show a heterotetramer
CC of 2 PCNA2 and 2 PCNA3, which would be large enough to clamp a Holliday
CC junction (PubMed:21352919). {ECO:0000250, ECO:0000269|PubMed:18782564,
CC ECO:0000269|PubMed:21352919}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000023; BAK54417.1; -; Genomic_DNA.
DR RefSeq; WP_010978940.1; NC_003106.2.
DR PDB; 3AIX; X-ray; 2.90 A; A=1-246.
DR PDB; 3AIZ; X-ray; 2.80 A; C/D=1-246.
DR PDBsum; 3AIX; -.
DR PDBsum; 3AIZ; -.
DR AlphaFoldDB; Q973F5; -.
DR SMR; Q973F5; -.
DR STRING; 273063.STK_09440; -.
DR GeneID; 1458909; -.
DR KEGG; sto:STK_09440; -.
DR PATRIC; fig|273063.9.peg.1056; -.
DR eggNOG; arCOG00488; Archaea.
DR OrthoDB; 14749at2157; -.
DR EvolutionaryTrace; Q973F5; -.
DR Proteomes; UP000001015; 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 CDD; cd00577; PCNA; 1.
DR Gene3D; 3.70.10.10; -; 1.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR InterPro; IPR046938; DNA_clamp_sf.
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; PROLIFERATING CELL NUCLEAR ANTIGEN; 1.
DR PANTHER; PTHR11352:SF0; PROLIFERATING CELL NUCLEAR ANTIGEN; 1.
DR Pfam; PF02747; PCNA_C; 1.
DR Pfam; PF00705; PCNA_N; 1.
DR PRINTS; PR00339; PCNACYCLIN.
DR SUPFAM; SSF55979; DNA clamp; 2.
DR PROSITE; PS01251; PCNA_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Reference proteome.
FT CHAIN 1..246
FT /note="DNA polymerase sliding clamp 3"
FT /id="PRO_0000149219"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:3AIZ"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 97..111
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3AIZ"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:3AIZ"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:3AIZ"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3AIZ"
SQ SEQUENCE 246 AA; 27437 MW; BA370A5D227B4E7F CRC64;
MRVKVIDADA FSYIFRTLEE FIDEITLDFT SDGLKIRGID PSRVTFIDIL IPAGYFEEYN
VEKEEKVGVK LEDFTDVLKT VTKNDSLYLE TDENQNIKVT LDGVYERTFT FPSIVASEIE
TPNLNLEFPF KAKALTVTFT DIIDEIEDIG GDSITFKAEG GKLYLSANSD MGSSTIELST
ENGGLLESEG GDAESVYGLE YVVNTSKMRK PSDTVEIAFG SQIPLKLRYN LPQGGYADFY
IAPRAE
//
