PCNA1_SULTO
ID PCNA1_SULTO Reviewed; 245 AA.
AC Q975N2; F9VMW4;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 118.
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;
GN OrderedLocusNames=STK_03870;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; 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 PCNA3, 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 (1.68 ANGSTROMS).
RA Tanabe E., Yasutake Y., Tanaka Y., Yao M., Tsumoto K., Kumagai I.,
RA Tanaka I.;
RT "Crystal structure of proliferating cell nuclear antigen (PCNA) homolog
RT from Sulfolobus tokodaii.";
RL Submitted (JUL-2011) to the PDB data bank.
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). The trimeric complex inhibits DNA ligase and both 3'-5'
CC and 5'-3' activity of Hel308 (Hjm) helicase, but stimulates 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 a dimeric complex with PCNA3 and a
CC trimeric complex with PCNA2 and PCNA3; does not form homotrimers
CC (PubMed:18782564). {ECO:0000250, ECO:0000269|PubMed:18782564}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
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DR EMBL; BA000023; BAK54261.1; -; Genomic_DNA.
DR RefSeq; WP_010978351.1; NC_003106.2.
DR PDB; 1UD9; X-ray; 1.68 A; A/B/C/D=2-245.
DR PDBsum; 1UD9; -.
DR AlphaFoldDB; Q975N2; -.
DR SMR; Q975N2; -.
DR STRING; 273063.STK_03870; -.
DR EnsemblBacteria; BAK54261; BAK54261; STK_03870.
DR GeneID; 1458312; -.
DR KEGG; sto:STK_03870; -.
DR PATRIC; fig|273063.9.peg.448; -.
DR eggNOG; arCOG00488; Archaea.
DR OMA; TIRKDPN; -.
DR OrthoDB; 70433at2157; -.
DR EvolutionaryTrace; Q975N2; -.
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 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; DNA replication; DNA-binding; Reference proteome.
FT CHAIN 1..245
FT /note="DNA polymerase sliding clamp 1"
FT /id="PRO_0000149217"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1UD9"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1UD9"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1UD9"
SQ SEQUENCE 245 AA; 27284 MW; BB73C45F8A83D91A CRC64;
MHIVYDDVRD LKAIIQALLK LVDEALFDIK PEGIQLVAID KAHISLIKIE LPKEMFKEYD
VPEEFKFGFN TQYMSKLLKA AKRKEEIIID ADSPEVVKLT LSGALNRVFN VNNIEVLPPE
VPEVNLEFDI KATINASGLK NAIGEIAEVA DTLLISGNEE KVVVKGEGEN KVEVEFSKDT
GSLADIEFNK ESSSAYDVEY LNDIISLTKL SDYVKVAFAD QKPMQLEFNM EGGGKVTYLL
APKLS
