PCNA1_SACS2
ID PCNA1_SACS2 Reviewed; 249 AA.
AC P57766;
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 1 {ECO:0000255|HAMAP-Rule:MF_00317};
DE AltName: Full=Proliferating cell nuclear antigen homolog 1 {ECO:0000255|HAMAP-Rule:MF_00317};
DE Short=PCNA1 {ECO:0000255|HAMAP-Rule:MF_00317};
GN Name=pcn1 {ECO:0000255|HAMAP-Rule:MF_00317}; Synonyms=pcnA-like;
GN OrderedLocusNames=SSO0397; ORFNames=C41_008;
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 FEN AND PCNA2, 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, INTERACTION WITH HJC, 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 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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PCNA2 AND FEN,
RP SUBUNIT, AND MUTAGENESIS OF 114-TYR--LYS-116 AND 175-LYS--TYR-177.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-249, 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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 3-249 IN COMPLEX WITH DPO4,
RP INTERACTION WITH DPO4, AND 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).
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.
CC Heterotrimer stimulates the Holliday junction resolvase Hjc. 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 {ECO:0000269|PubMed:12535540, ECO:0000269|PubMed:17011573}.
CC -!- SUBUNIT: Forms heterodimers with PCNA2, which then recruit PCNA3; does
CC not form homotrimers (PubMed:12535540, PubMed:18703842). The
CC heterodimers interact with RfcS homotetramers (PubMed:12535540).
CC Heterotrimer which circularizes head-to-tail (head is at N-terminus,
CC tail is at C-terminus) to form a toroid; DNA passes through its center.
CC Replication factor C (RFC) is required to load the toroid on the DNA.
CC Heterotrimer interacts, probably via this subunit, with flap
CC endonuclease 1 (fen) (PubMed:12535540), Hjc (PubMed:17011573), Dpo4
CC (PubMed:19054331), and XPF (PubMed:12675797).
CC {ECO:0000269|PubMed:12535540, ECO:0000269|PubMed:12675797,
CC ECO:0000269|PubMed:16945955, ECO:0000269|PubMed:17011573,
CC ECO:0000269|PubMed:17012780, ECO:0000269|PubMed:17052461,
CC ECO:0000269|PubMed:18703842, ECO:0000269|PubMed:19054331}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
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DR EMBL; AE006641; AAK40726.1; -; Genomic_DNA.
DR PIR; G90183; G90183.
DR RefSeq; WP_009988793.1; NC_002754.1.
DR PDB; 2HII; X-ray; 2.79 A; A/X=1-249.
DR PDB; 2HIK; X-ray; 3.30 A; A/L/X=1-249.
DR PDB; 2IO4; X-ray; 2.60 A; A/C=1-249.
DR PDB; 2IX2; X-ray; 2.20 A; A=1-249.
DR PDB; 2IZO; X-ray; 2.90 A; C=1-249.
DR PDB; 2NTI; X-ray; 2.50 A; A/D/G=1-249.
DR PDB; 3FDS; X-ray; 2.05 A; C=1-249.
DR PDB; 7RPO; EM; 4.16 A; A=2-249.
DR PDB; 7RPW; EM; 4.38 A; A=2-249.
DR PDB; 7RPX; EM; 4.20 A; A=2-249.
DR PDBsum; 2HII; -.
DR PDBsum; 2HIK; -.
DR PDBsum; 2IO4; -.
DR PDBsum; 2IX2; -.
DR PDBsum; 2IZO; -.
DR PDBsum; 2NTI; -.
DR PDBsum; 3FDS; -.
DR PDBsum; 7RPO; -.
DR PDBsum; 7RPW; -.
DR PDBsum; 7RPX; -.
DR AlphaFoldDB; P57766; -.
DR SMR; P57766; -.
DR DIP; DIP-48854N; -.
DR IntAct; P57766; 1.
DR STRING; 273057.SSO0397; -.
DR EnsemblBacteria; AAK40726; AAK40726; SSO0397.
DR GeneID; 44129378; -.
DR KEGG; sso:SSO0397; -.
DR PATRIC; fig|273057.12.peg.393; -.
DR eggNOG; arCOG00488; Archaea.
DR HOGENOM; CLU_043978_1_0_2; -.
DR InParanoid; P57766; -.
DR OMA; NASKMKY; -.
DR PhylomeDB; P57766; -.
DR EvolutionaryTrace; P57766; -.
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; IPR022648; Pr_cel_nuc_antig_N.
DR PANTHER; PTHR11352:SF0; PTHR11352:SF0; 1.
DR Pfam; PF00705; PCNA_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication; DNA-binding;
KW Reference proteome.
FT CHAIN 1..249
FT /note="DNA polymerase sliding clamp 1"
FT /id="PRO_0000149215"
FT MUTAGEN 114..116
FT /note="YIK->ELE: Loss of interaction with PCNA3, no change
FT with PCNA2."
FT /evidence="ECO:0000269|PubMed:16945955"
FT MUTAGEN 175..177
FT /note="KRY->EED: Loss of interaction with both PCNA3 and
FT PCNA2."
FT /evidence="ECO:0000269|PubMed:16945955"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3FDS"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:3FDS"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:3FDS"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3FDS"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:3FDS"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2NTI"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3FDS"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3FDS"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:3FDS"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:3FDS"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3FDS"
SQ SEQUENCE 249 AA; 27536 MW; 137EB10BE2C03F77 CRC64;
MFKIVYPNAK DFFSFINSIT NVTDSIILNF TEDGIFSRHL TEDKVLMAIM RIPKDVLSEY
SIDSPTSVKL DVSSVKKILS KASSKKATIE LTETDSGLKI IIRDEKSGAK STIYIKAEKG
QVEQLTEPKV NLAVNFTTDE SVLNVIAADV TLVGEEMRIS TEEDKIKIEA GEEGKRYVAF
LMKDKPLKEL SIDTSASSSY SAEMFKDAVK GLRGFSAPTM VSFGENLPMK IDVEAVSGGH
MIFWIAPRL
