ID   CDC18_SCHPO             Reviewed;         577 AA.
AC   P41411;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Cell division control protein 18;
GN   Name=cdc18; ORFNames=SPBC14C8.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=7916658; DOI=10.1016/0092-8674(93)90427-r;
RA   Kelly T.J., Martin G.S., Forsburg S.L., Stephen R.J., Russo A., Nurse P.;
RT   "The fission yeast cdc18+ gene product couples S phase to START and
RT   mitosis.";
RL   Cell 74:371-382(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=8521469; DOI=10.1016/0092-8674(95)90117-5;
RA   Nishitani H., Nurse P.;
RT   "p65cdc18 plays a major role controlling the initiation of DNA replication
RT   in fission yeast.";
RL   Cell 83:397-405(1995).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH POP1.
RX   PubMed=9203581; DOI=10.1101/gad.11.12.1548;
RA   Kominami K., Toda T.;
RT   "Fission yeast WD-repeat protein pop1 regulates genome ploidy through
RT   ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the
RT   S-phase initiator Cdc18.";
RL   Genes Dev. 11:1548-1560(1997).
RN   [5]
RP   INTERACTION WITH POP2.
RX   PubMed=9653157; DOI=10.1073/pnas.95.14.8159;
RA   Jallepalli P.V., Tien D., Kelly T.J.;
RT   "sud1+ targets cyclin-dependent kinase-phosphorylated Cdc18 and Rum1
RT   proteins for degradation and stops unwanted diploidization in fission
RT   yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8159-8164(1998).
RN   [6]
RP   INTERACTION WITH POP1 AND POP2.
RX   PubMed=10209119; DOI=10.1016/s0960-9822(99)80165-1;
RA   Wolf D.A., McKeon F., Jackson P.K.;
RT   "F-box/WD-repeat proteins pop1p and Sud1p/Pop2p form complexes that bind
RT   and direct the proteolysis of cdc18p.";
RL   Curr. Biol. 9:373-376(1999).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH CDT1.
RX   PubMed=10766248; DOI=10.1038/35007110;
RA   Nishitani H., Lygerou Z., Nishimoto T., Nurse P.;
RT   "The Cdt1 protein is required to license DNA for replication in fission
RT   yeast.";
RL   Nature 404:625-628(2000).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF THR-27; THR-98; THR-104 AND THR-134.
RX   PubMed=11486016; DOI=10.1128/mcb.21.17.5767-5777.2001;
RA   Vas A., Mok W., Leatherwood J.;
RT   "Control of DNA rereplication via Cdc2 phosphorylation sites in the origin
RT   recognition complex.";
RL   Mol. Cell. Biol. 21:5767-5777(2001).
RN   [9]
RP   INTERACTION WITH ORC.
RX   PubMed=11850415; DOI=10.1074/jbc.m107710200;
RA   Chuang R.-Y., Chretien L., Dai J., Kelly T.J.;
RT   "Purification and characterization of the Schizosaccharomyces pombe origin
RT   recognition complex: interaction with origin DNA and Cdc18 protein.";
RL   J. Biol. Chem. 277:16920-16927(2002).
RN   [10]
RP   FUNCTION.
RX   PubMed=11988741; DOI=10.1038/ncb789;
RA   Murakami H., Yanow S.K., Griffiths D., Nakanishi M., Nurse P.;
RT   "Maintenance of replication forks and the S-phase checkpoint by Cdc18p and
RT   Orp1p.";
RL   Nat. Cell Biol. 4:384-388(2002).
CC   -!- FUNCTION: Part of the checkpoint control that prevents mitosis from
CC       occurring until S phase is completed. Plays a key role in coupling S
CC       phase to start and mitosis. Acts at the initiation of DNA replication
CC       and plays a major role in controlling the onset of S-phase. Together
CC       with orc1, involved in the maintenance of replication forks and
CC       activation of cds1-dependent S-phase checkpoint. Together with orc2,
CC       plays a role in preventing DNA rereplication and resulting genetic
CC       instability (PubMed:11486016). {ECO:0000269|PubMed:10766248,
CC       ECO:0000269|PubMed:11486016, ECO:0000269|PubMed:11988741,
CC       ECO:0000269|PubMed:7916658, ECO:0000269|PubMed:8521469,
CC       ECO:0000269|PubMed:9203581}.
CC   -!- SUBUNIT: Interacts with the origin recognition complex (ORC) and is
CC       recruited to the ars1 origin of replication. Interacts with cdt1, pop1
CC       and pop2. {ECO:0000269|PubMed:10209119, ECO:0000269|PubMed:10766248,
CC       ECO:0000269|PubMed:11850415, ECO:0000269|PubMed:9203581,
CC       ECO:0000269|PubMed:9653157}.
CC   -!- INTERACTION:
CC       P41411; P87060: pop1; NbExp=3; IntAct=EBI-1207853, EBI-1185389;
CC       P41411; O14170: pop2; NbExp=3; IntAct=EBI-1207853, EBI-1185414;
CC   -!- PTM: Ubiquitinated by pop1 and pop2 and targeted to the 26S proteasome
CC       for degradation.
CC   -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000305}.
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DR   EMBL; L16793; AAA02871.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA18425.1; -; Genomic_DNA.
DR   PIR; A40726; A40726.
DR   RefSeq; NP_595910.1; NM_001021818.2.
DR   AlphaFoldDB; P41411; -.
DR   SMR; P41411; -.
DR   BioGRID; 276557; 56.
DR   IntAct; P41411; 3.
DR   STRING; 284812.P41411; -.
DR   iPTMnet; P41411; -.
DR   PaxDb; 4896-SPBC14C8-07c-1; -.
DR   EnsemblFungi; SPBC14C8.07c.1; SPBC14C8.07c.1:pep; SPBC14C8.07c.
DR   GeneID; 2540013; -.
DR   KEGG; spo:SPBC14C8.07c; -.
DR   PomBase; SPBC14C8.07c; cdc18.
DR   VEuPathDB; FungiDB:SPBC14C8.07c; -.
DR   eggNOG; KOG2227; Eukaryota.
DR   HOGENOM; CLU_012774_2_0_1; -.
DR   InParanoid; P41411; -.
DR   OMA; LFEWSLH; -.
DR   PhylomeDB; P41411; -.
DR   Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-SPO-68689; CDC6 association with the ORC:origin complex.
DR   Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR   Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR   Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   PRO; PR:P41411; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; ISO:PomBase.
DR   GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0140530; P:MCM complex loading; IMP:PomBase.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IGI:PomBase.
DR   GO; GO:1902985; P:mitotic pre-replicative complex assembly; ISO:PomBase.
DR   GO; GO:1903468; P:positive regulation of DNA replication initiation; IMP:PomBase.
DR   GO; GO:1905634; P:regulation of protein localization to chromatin; IMP:PomBase.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd08768; Cdc6_C; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041083; AAA_lid_10.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR016314; Cdc6/18.
DR   InterPro; IPR015163; Cdc6_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10763:SF26; CELL DIVISION CONTROL PROTEIN 6 HOMOLOG; 1.
DR   PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17872; AAA_lid_10; 1.
DR   Pfam; PF09079; Cdc6_C; 1.
DR   PIRSF; PIRSF001767; Cdc6; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01074; Cdc6_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; DNA replication; Mitosis;
KW   Nucleotide-binding; Reference proteome; Ubl conjugation.
FT   CHAIN           1..577
FT                   /note="Cell division control protein 18"
FT                   /id="PRO_0000150978"
FT   REGION          30..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         199..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         27
FT                   /note="T->A: Enhanced rereplication in orc2 mutant lacking
FT                   four cdc2 phosphorylation sites; when associated with A-98;
FT                   A-104 and A-134."
FT                   /evidence="ECO:0000269|PubMed:11486016"
FT   MUTAGEN         98
FT                   /note="T->A: Enhanced rereplication in orc2 mutant lacking
FT                   four cdc2 phosphorylation sites; when associated with A-27;
FT                   A-104 and A-134."
FT                   /evidence="ECO:0000269|PubMed:11486016"
FT   MUTAGEN         104
FT                   /note="T->A: Enhanced rereplication in orc2 mutant lacking
FT                   four cdc2 phosphorylation sites; when associated with A-27;
FT                   A-98 and A-134."
FT                   /evidence="ECO:0000269|PubMed:11486016"
FT   MUTAGEN         134
FT                   /note="T->A: Enhanced rereplication in orc2 mutant lacking
FT                   four cdc2 phosphorylation sites; when associated with A-27;
FT                   A-98 and A-104."
FT                   /evidence="ECO:0000269|PubMed:11486016"
SQ   SEQUENCE   577 AA;  64753 MW;  74DBE9D5CF23504D CRC64;
     MCETPIGCHT PRRCNRFIDS AALIDCTNKT NQREHSPSFS IEIPTTPSRK RTLASSHFQT
     PTKRIKYELG ELQEEKTDLY PNFPAQLKEN KKPKLPTTPQ TPKTPKRTIQ IVTPKSLNRT
     CNPVPFATRL LQSTPHRQLF PPTPSTPSTP SYNSTAKLSL RKSYRSAGVV GRENEKSIVE
     SFFRQHLDAN AGGALYVSGA PGTGKTVLLH NVLDHVVSDY PKVNVCYINC MTINEPKAIF
     EKIHSKIVKE EILENEDHHI NFQCELESHF TQSANELYNP VIIVLDEMDH LIAREQQVLY
     TLFEWPSRPT SRLILVGIAN ALDMTDRFLP RLRTKHITPK LLSFTPYTAQ EISTIIKARL
     KTAATTSEKN NPFTPIKSIS EVSDDSINVV SQHADETPFI HPAAIELCAR KVAASSGDLR
     KALDICRHAI ELAEREWKAQ HDNTLSSVDI PRASIAHVVR ATSAMSQSAS ARLKNLGLQQ
     KAILCTLVVC EKTSLSVADV FEKYSSLCLR DRLIYPLTSS EFCDVANSLE TLAIIRLRTK
     QRNGKPQDRI ISLLVPEMDV ITAVGDIGTL KRFFDRR
//