PCNA3_SACS2
ID PCNA3_SACS2 Reviewed; 244 AA.
AC P57765;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
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=pcnA-1;
GN OrderedLocusNames=SSO0405; ORFNames=C41_016;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10438605; DOI=10.1006/jmbi.1999.2939;
RA De Felice M., Sensen C.W., Charlebois R.L., Rossi M., Pisani F.M.;
RT "Two DNA polymerase sliding clamps from the thermophilic archaeon
RT Sulfolobus solfataricus.";
RL J. Mol. Biol. 291:47-57(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, INTERACTION WITH DPO1; LIG AND RFCL, AND SUBUNIT.
RX PubMed=12535540; DOI=10.1016/s1097-2765(02)00824-9;
RA Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D.;
RT "A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus
RT solfataricus.";
RL Mol. Cell 11:275-282(2003).
RN [4]
RP INTERACTION WITH XPF, AND SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12675797; DOI=10.1046/j.1365-2958.2003.03444.x;
RA Roberts J.A., Bell S.D., White M.F.;
RT "An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA.";
RL Mol. Microbiol. 48:361-371(2003).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17011573; DOI=10.1016/j.jmb.2006.09.011;
RA Dorazi R., Parker J.L., White M.F.;
RT "PCNA activates the Holliday junction endonuclease Hjc.";
RL J. Mol. Biol. 364:243-247(2006).
RN [6]
RP SUBUNIT.
RX PubMed=16945955; DOI=10.1093/nar/gkl623;
RA Dore A.S., Kilkenny M.L., Jones S.A., Oliver A.W., Roe S.M., Bell S.D.,
RA Pearl L.H.;
RT "Structure of an archaeal PCNA1-PCNA2-FEN1 complex: elucidating PCNA
RT subunit and client enzyme specificity.";
RL Nucleic Acids Res. 34:4515-4526(2006).
RN [7]
RP SUBUNIT.
RX PubMed=19054331; DOI=10.1111/j.1365-2958.2008.06553.x;
RA Xing G., Kirouac K., Shin Y.J., Bell S.D., Ling H.;
RT "Structural insight into recruitment of translesion DNA polymerase Dpo4 to
RT sliding clamp PCNA.";
RL Mol. Microbiol. 71:678-691(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND SUBUNIT.
RX PubMed=17012780; DOI=10.1107/s1744309106034075;
RA Williams G.J., Johnson K., Rudolf J., McMahon S.A., Carter L., Oke M.,
RA Liu H., Taylor G.L., White M.F., Naismith J.H.;
RT "Structure of the heterotrimeric PCNA from Sulfolobus solfataricus.";
RL Acta Crystallogr. F 62:944-948(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS), AND SUBUNIT.
RX PubMed=17052461; DOI=10.1016/j.molcel.2006.08.015;
RA Pascal J.M., Tsodikov O.V., Hura G.L., Song W., Cotner E.A., Classen S.,
RA Tomkinson A.E., Tainer J.A., Ellenberger T.;
RT "A flexible interface between DNA ligase and PCNA supports conformational
RT switching and efficient ligation of DNA.";
RL Mol. Cell 24:279-291(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=18703842; DOI=10.1107/s0907444908021665;
RA Hlinkova V., Xing G., Bauer J., Shin Y.J., Dionne I., Rajashankar K.R.,
RA Bell S.D., Ling H.;
RT "Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and
RT opening.";
RL Acta Crystallogr. D 64:941-949(2008).
CC -!- FUNCTION: One of the sliding clamp subunits that acts as a moving
CC platform for DNA processing. Responsible for tethering the catalytic
CC subunit of DNA polymerase to DNA during high-speed replication. DNA
CC polymerase I, DNA ligase and the flap endonuclease may be
CC constitutively associated with the PCNA heterotrimer forming a scanning
CC complex able to couple DNA synthesis and Okazaki fragment maturation.
CC Heterotrimer stimulates the Holliday junction resolvase Hjc.
CC {ECO:0000269|PubMed:12535540, ECO:0000269|PubMed:17011573}.
CC -!- SUBUNIT: Does not individually interact with either of the other PCNA
CC subunits, but is recruited to a PCNA1-PCNA2 heterodimer; does not form
CC homotrimers (PubMed:12535540, PubMed:18703842). Heterotrimer which
CC circularizes head-to-tail (head is at N-terminus, tail is at C-
CC terminus) to form a toroid; DNA passes through its center. Replication
CC factor C (RFC) is required to load the toroid on the DNA. This subunit
CC interacts with DNA ligase, RfcL, XPF, and weakly with DNA polymerase I
CC (PubMed:12535540). {ECO:0000269|PubMed:12535540,
CC ECO:0000269|PubMed:12675797, ECO:0000269|PubMed:16945955,
CC ECO:0000269|PubMed:17011573, ECO:0000269|PubMed:17012780,
CC ECO:0000269|PubMed:17052461, ECO:0000269|PubMed:18703842,
CC ECO:0000269|PubMed:19054331}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40734.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AE006641; AAK40734.1; ALT_INIT; Genomic_DNA.
DR PIR; G90184; G90184.
DR PDB; 2HII; X-ray; 2.79 A; C/Z=1-244.
DR PDB; 2HIK; X-ray; 3.30 A; C/N/Z=1-244.
DR PDB; 2IJX; X-ray; 1.90 A; A/B/C/D=1-244.
DR PDB; 2IX2; X-ray; 2.20 A; C=1-244.
DR PDB; 2NTI; X-ray; 2.50 A; C/F/I=1-244.
DR PDB; 7RPO; EM; 4.16 A; C=1-244.
DR PDB; 7RPW; EM; 4.38 A; C=1-244.
DR PDB; 7RPX; EM; 4.20 A; C=1-244.
DR PDBsum; 2HII; -.
DR PDBsum; 2HIK; -.
DR PDBsum; 2IJX; -.
DR PDBsum; 2IX2; -.
DR PDBsum; 2NTI; -.
DR PDBsum; 7RPO; -.
DR PDBsum; 7RPW; -.
DR PDBsum; 7RPX; -.
DR AlphaFoldDB; P57765; -.
DR SMR; P57765; -.
DR STRING; 273057.SSO0405; -.
DR EnsemblBacteria; AAK40734; AAK40734; SSO0405.
DR KEGG; sso:SSO0405; -.
DR PATRIC; fig|273057.12.peg.401; -.
DR eggNOG; arCOG00488; Archaea.
DR HOGENOM; CLU_043978_1_0_2; -.
DR InParanoid; P57765; -.
DR OMA; TIRKDPN; -.
DR PhylomeDB; P57765; -.
DR EvolutionaryTrace; P57765; -.
DR Proteomes; UP000001974; 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; 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; Direct protein sequencing; DNA replication; DNA-binding;
KW Reference proteome.
FT CHAIN 1..244
FT /note="DNA polymerase sliding clamp 3"
FT /id="PRO_0000149214"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2IJX"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:2IJX"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2IJX"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 96..112
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2IJX"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:2IJX"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2IJX"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:2IJX"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:2IJX"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:2IJX"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2IJX"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2IJX"
SQ SEQUENCE 244 AA; 27459 MW; 191C3C1267F1F5D1 CRC64;
MKVVYDDVRV LKDIIQALAR LVDEAVLKFK QDSVELVALD RAHISLISVN LPREMFKEYD
VNDEFKFGFN TQYLMKILKV AKRKEAIEIA SESPDSVIIN IIGSTNREFN VRNLEVSEQE
IPEINLQFDI SATISSDGFK SAISEVSTVT DNVVVEGHED RILIKAEGES EVEVEFSKDT
GGLQDLEFSK ESKNSYSAEY LDDVLSLTKL SDYVKISFGN QKPLQLFFNM EGGGKVTYLL
APKV
