ID   TIP_THEKO               Reviewed;          64 AA.
AC   Q5JH72;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=PCNA-inhibitor {ECO:0000305};
DE   AltName: Full=Thermococcales inhibitor of PCNA {ECO:0000303|PubMed:24728986};
DE            Short=TIP {ECO:0000303|PubMed:24728986};
GN   OrderedLocusNames=TK0808 {ECO:0000312|EMBL:BAD84997.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH PCN1 AND PCN2.
RX   PubMed=24728986; DOI=10.1093/nar/gku239;
RA   Li Z., Huang R.Y., Yopp D.C., Hileman T.H., Santangelo T.J., Hurwitz J.,
RA   Hudgens J.W., Kelman Z.;
RT   "A novel mechanism for regulating the activity of proliferating cell
RT   nuclear antigen by a small protein.";
RL   Nucleic Acids Res. 42:5776-5789(2014).
RN   [3] {ECO:0007744|PDB:5DA7}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH PCNA 1, FUNCTION,
RP   AND PIP MOTIF.
RX   PubMed=27141962; DOI=10.1093/nar/gkw351;
RA   Altieri A.S., Ladner J.E., Li Z., Robinson H., Sallman Z.F., Marino J.P.,
RA   Kelman Z.;
RT   "A small protein inhibits proliferating cell nuclear antigen by breaking
RT   the DNA clamp.";
RL   Nucleic Acids Res. 44:6232-6241(2016).
CC   -!- FUNCTION: Binds to the DNA polymerase sliding clamp (PCNA) and
CC       dissociates the PCNA trimeric ring, leading to the inhibition of PCNA-
CC       dependent activities (PubMed:24728986, PubMed:27141962). In vitro,
CC       inhibits the PCNA-dependent activities of DNA polymerase PolB and of
CC       flap endonuclease 1 (FEN-1) (PubMed:24728986).
CC       {ECO:0000269|PubMed:24728986, ECO:0000269|PubMed:27141962}.
CC   -!- SUBUNIT: Interacts with PCNA via a non-canonical PIP (PCNA-interacting
CC       peptide) motif. Can bind both Pcn1 and Pcn2.
CC       {ECO:0000269|PubMed:24728986, ECO:0000269|PubMed:27141962}.
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DR   EMBL; AP006878; BAD84997.1; -; Genomic_DNA.
DR   RefSeq; WP_011249759.1; NC_006624.1.
DR   PDB; 5DA7; X-ray; 2.80 A; B/E=1-64.
DR   PDBsum; 5DA7; -.
DR   AlphaFoldDB; Q5JH72; -.
DR   SMR; Q5JH72; -.
DR   STRING; 69014.TK0808; -.
DR   EnsemblBacteria; BAD84997; BAD84997; TK0808.
DR   GeneID; 3234016; -.
DR   KEGG; tko:TK0808; -.
DR   PATRIC; fig|69014.16.peg.788; -.
DR   eggNOG; arCOG05824; Archaea.
DR   HOGENOM; CLU_2802469_0_0_2; -.
DR   OMA; PEEHINY; -.
DR   OrthoDB; 129360at2157; -.
DR   Proteomes; UP000000536; Chromosome.
DR   DisProt; DP00915; -.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome.
FT   CHAIN           1..64
FT                   /note="PCNA-inhibitor"
FT                   /id="PRO_0000442529"
FT   MOTIF           31..38
FT                   /note="PIP motif"
FT                   /evidence="ECO:0000305|PubMed:27141962"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:5DA7"
FT   HELIX           40..55
FT                   /evidence="ECO:0007829|PDB:5DA7"
SQ   SEQUENCE   64 AA;  7611 MW;  AF5971AFB582A564 CRC64;
     MDRKLDEFIG DATPKKVSKE KPVRRKKRLK PTSLDSFLPE EHINYFRDLR IGSKKIRNAK
     IEEL