PCNA_PYRAB
ID PCNA_PYRAB Reviewed; 249 AA.
AC Q9UYX8; G8ZHI5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=PYRAB13790;
GN ORFNames=PAB1465;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP INTERACTION WITH NUCS.
RX PubMed=19609302; DOI=10.1038/emboj.2009.192;
RA Ren B., Kuhn J., Meslet-Cladiere L., Briffotaux J., Norais C., Lavigne R.,
RA Flament D., Ladenstein R., Myllykallio H.;
RT "Structure and function of a novel endonuclease acting on branched DNA
RT substrates.";
RL EMBO J. 28:2479-2489(2009).
RN [4]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH NUCS.
RX PubMed=22431731; DOI=10.1074/jbc.m112.346361;
RA Creze C., Ligabue A., Laurent S., Lestini R., Laptenok S.P., Kuhn J.,
RA Vos M.H., Czjzek M., Myllykallio H., Flament D.;
RT "Modulation of the Pyrococcus abyssi NucS endonuclease activity by the
RT replication clamp PCNA at functional and structural levels.";
RL J. Biol. Chem. 287:15648-15660(2012).
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). Regulates activity of NucS endonuclease and prevents non-
CC specific cleavage. {ECO:0000255|HAMAP-Rule:MF_00317,
CC ECO:0000269|PubMed:22431731}.
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). Homotrimer. Interacts with NucS.
CC {ECO:0000250, ECO:0000269|PubMed:19609302,
CC ECO:0000269|PubMed:22431731}.
CC -!- INTERACTION:
CC Q9UYX8; Q9V2E8: nucS; NbExp=3; IntAct=EBI-7103152, EBI-7103178;
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
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DR EMBL; AJ248287; CAB50284.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70822.1; -; Genomic_DNA.
DR PIR; G75048; G75048.
DR RefSeq; WP_010868494.1; NC_000868.1.
DR PDB; 6T7X; X-ray; 2.30 A; A=1-249.
DR PDB; 6T7Y; X-ray; 2.70 A; A=1-249.
DR PDB; 6T8H; EM; 3.77 A; C/D/E=1-249.
DR PDBsum; 6T7X; -.
DR PDBsum; 6T7Y; -.
DR PDBsum; 6T8H; -.
DR AlphaFoldDB; Q9UYX8; -.
DR SMR; Q9UYX8; -.
DR IntAct; Q9UYX8; 1.
DR MINT; Q9UYX8; -.
DR STRING; 272844.PAB1465; -.
DR EnsemblBacteria; CAB50284; CAB50284; PAB1465.
DR GeneID; 1496768; -.
DR KEGG; pab:PAB1465; -.
DR PATRIC; fig|272844.11.peg.1465; -.
DR eggNOG; arCOG00488; Archaea.
DR HOGENOM; CLU_043978_1_1_2; -.
DR OMA; TIRKDPN; -.
DR OrthoDB; 70433at2157; -.
DR PhylomeDB; Q9UYX8; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..249
FT /note="DNA polymerase sliding clamp"
FT /id="PRO_0000149203"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6T7X"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:6T7X"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6T7X"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 95..114
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:6T7X"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:6T7X"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:6T7X"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6T7X"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:6T7X"
SQ SEQUENCE 249 AA; 28035 MW; B7E21A135B3F3BC8 CRC64;
MPFEIVFEGA KEFAQLIETA SRLIDEAAFK VTEEGISMRA MDPSRVVLID LNLPASIFSK
YEVDGEETIG VNMDHLKKVL KRGKAKETLI LRKGEENFLE ISLQGTATRT FKLPLIDVEE
IEVDLPELPF TAKVVILGDV IKEAVKDASL VSDSMKFIAK ENEFTMRAEG ETQEVEVKLT
LEDEGLLDIE VQEETKSAYG ISYLSDMVKG LGKADEVTIK FGNEMPMQME YYIRDEGRLI
FLLAPRVEE
