PCNA2_SULTO
ID PCNA2_SULTO Reviewed; 248 AA.
AC Q975M2; F9VMW8;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=DNA polymerase sliding clamp 2 {ECO:0000255|HAMAP-Rule:MF_00317};
DE AltName: Full=Proliferating cell nuclear antigen homolog 2 {ECO:0000255|HAMAP-Rule:MF_00317};
DE Short=PCNA2 {ECO:0000255|HAMAP-Rule:MF_00317};
GN Name=pcn2 {ECO:0000255|HAMAP-Rule:MF_00317}; Synonyms=pcnB;
GN OrderedLocusNames=STK_03970;
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 (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 a dimeric complex with PCNA3 and
CC trimeric complexes PCNA123 and PCNA323; does not form homotrimers
CC (PubMed:18782564). Crystal structures show a heterotetramer of 2 PCNA2
CC and 2 PCNA3, which would be large enough to clamp a Holliday junction
CC (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}.
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DR EMBL; BA000023; BAK54265.1; -; Genomic_DNA.
DR RefSeq; WP_010978361.1; NC_003106.2.
DR PDB; 3AIX; X-ray; 2.90 A; B=1-248.
DR PDB; 3AIZ; X-ray; 2.80 A; A/B=1-248.
DR PDBsum; 3AIX; -.
DR PDBsum; 3AIZ; -.
DR AlphaFoldDB; Q975M2; -.
DR SMR; Q975M2; -.
DR STRING; 273063.STK_03970; -.
DR EnsemblBacteria; BAK54265; BAK54265; STK_03970.
DR GeneID; 1458322; -.
DR KEGG; sto:STK_03970; -.
DR PATRIC; fig|273063.9.peg.458; -.
DR eggNOG; arCOG00488; Archaea.
DR OMA; NASKMKY; -.
DR OrthoDB; 70433at2157; -.
DR EvolutionaryTrace; Q975M2; -.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Reference proteome.
FT CHAIN 1..248
FT /note="DNA polymerase sliding clamp 2"
FT /id="PRO_0000149218"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:3AIZ"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:3AIZ"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:3AIZ"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3AIZ"
SQ SEQUENCE 248 AA; 27542 MW; A19A2FB039874BB6 CRC64;
MIKATYSSAK DFYSLLSGLL KVTDEIILNF TEDSIFSRYL TDDKVLMVIF KIPKEYLEDY
TIDKPLGIKI NINDLKKILG KAKSKSATVT LEETEAGLKV TVRDEKTGTR SNIYIKGEKT
SIDQLTEPKV NLSVTFTTDG DVLKDIARDL SLVGEEVEIS ADENTVTLST EEAGRTYKSL
LKQDKPLKSL NVESPSKAVY SIEVLKDVFK VTSISQNVTV GFGNNIPMKI EVPTDSGGQL
IFWIAPRL
