CDC1_YEAST
ID CDC1_YEAST Reviewed; 491 AA.
AC P40986; D6VSG5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cell division control protein 1;
DE EC=3.1.-.-;
GN Name=CDC1; Synonyms=DSR1, ESP2; OrderedLocusNames=YDR182W;
GN ORFNames=YD9395.16;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / YPH1;
RX PubMed=7969142; DOI=10.1128/mcb.14.12.8037-8050.1994;
RA Halbrook J., Hoekstra M.F.;
RT "Mutations in the Saccharomyces cerevisiae CDC1 gene affect double-strand-
RT break-induced intrachromosomal recombination.";
RL Mol. Cell. Biol. 14:8037-8050(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200060 / W303;
RA Supek F., Supekova L., Nelson H., Nelson N.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Probable metallophosphoesterase which may participate in
CC recombinational repair of double -strand breaks.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 583 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1
CC family. {ECO:0000305}.
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DR EMBL; X81813; CAA57411.1; -; Genomic_DNA.
DR EMBL; U15970; AAB08444.1; -; Genomic_DNA.
DR EMBL; Z46727; CAA86689.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12025.1; -; Genomic_DNA.
DR PIR; S49779; S49779.
DR RefSeq; NP_010468.1; NM_001180490.1.
DR AlphaFoldDB; P40986; -.
DR BioGRID; 32236; 976.
DR IntAct; P40986; 2.
DR MINT; P40986; -.
DR STRING; 4932.YDR182W; -.
DR iPTMnet; P40986; -.
DR MaxQB; P40986; -.
DR PaxDb; P40986; -.
DR PRIDE; P40986; -.
DR EnsemblFungi; YDR182W_mRNA; YDR182W; YDR182W.
DR GeneID; 851763; -.
DR KEGG; sce:YDR182W; -.
DR SGD; S000002590; CDC1.
DR VEuPathDB; FungiDB:YDR182W; -.
DR eggNOG; KOG3662; Eukaryota.
DR GeneTree; ENSGT00390000013236; -.
DR HOGENOM; CLU_011607_0_0_1; -.
DR InParanoid; P40986; -.
DR OMA; SRTLHCM; -.
DR BioCyc; YEAST:G3O-29771-MON; -.
DR PRO; PR:P40986; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40986; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IGI:SGD.
DR CDD; cd08163; MPP_Cdc1; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041834; MPP_Cdc1.
DR InterPro; IPR033308; PGAP5/Cdc1/Ted1.
DR PANTHER; PTHR13315; PTHR13315; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Cell division control protein 1"
FT /id="PRO_0000089444"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..491
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 439
FT /note="P -> A (in Ref. 1; CAA57411)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="V -> G (in Ref. 1; CAA57411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 57147 MW; AE435F7DFDD7E2AE CRC64;
MVYRNRSKSV LSTHSKKSDD KAHYKSRSKK KSKSRSKKRL RIYWRYISIV WILWLGLISY
YESVVVKRAM KKCQWSTWED WPEGAESHRV GLFADPQIMD EYSYPGRPQI VNYFTRVIVD
HYHRRNWKYV QYYLDPDSNF FLGDLFDGGR NWDDKQWIKE YTRFNQIFPK KPLRRTVMSL
PGNHDIGFGD TVVESSLQRF SSYFGETSSS LDAGNHTFVL LDTISLSDKT NPNVSRVPRQ
FLDNFAMGSH PLPRILLTHV PLWRDPEQQT CGQLRESKEP FPIQKGHQYQ TVIENDISQE
ILTKIQPEIL FSGDDHDHCQ ISHSYPFQGK TKNAQEITVK SCAMNMGISR PAIQLLSLYN
PSDLTMVNAG GEYASKTYQT ELCYMPDPYK AIRMYLWGLL FSAAFIAYMH FFPKSFNNRV
ATIMNRVFTR PDGNTSDLPL PTSISKSKSK KSLTHSKYAV NDTRSIKQFL VNAIVLFVSV
MPIFIYFYTV V
