ID   CDC3_CANAX              Reviewed;         416 AA.
AC   P39826;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cell division control protein 3;
GN   Name=CDC3;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C792;
RX   PubMed=8152419; DOI=10.1007/bf00283424;
RA   Didomenico B.J., Brown N.H., Lupisella J., Greene J.R., Yanko M.,
RA   Koltin Y.;
RT   "Homologs of the yeast neck filament associated genes: isolation and
RT   sequence analysis of Candida albicans CDC3 and CDC10.";
RL   Mol. Gen. Genet. 242:689-698(1994).
CC   -!- FUNCTION: Plays a role in the cell cycle. Involved in the formation of
CC       the ring of filaments in the neck region at the mother-bud junction
CC       during mitosis.
CC   -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000250}. Note=Present at the bud
CC       neck during cell division. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01056}.
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DR   EMBL; Z25869; CAA81089.1; -; Genomic_DNA.
DR   PIR; S43279; S43279.
DR   AlphaFoldDB; P39826; -.
DR   SMR; P39826; -.
DR   VEuPathDB; FungiDB:C1_04210C_A; -.
DR   VEuPathDB; FungiDB:CAWG_00972; -.
DR   GO; GO:0005619; C:ascospore wall; IEA:EnsemblFungi.
DR   GO; GO:1990317; C:Gin4 complex; IEA:EnsemblFungi.
DR   GO; GO:0001400; C:mating projection base; IEA:EnsemblFungi.
DR   GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR   GO; GO:0031105; C:septin complex; IEA:EnsemblFungi.
DR   GO; GO:0032160; C:septin filament array; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:EnsemblFungi.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0000921; P:septin ring assembly; IEA:EnsemblFungi.
DR   GO; GO:0031107; P:septin ring disassembly; IEA:EnsemblFungi.
DR   CDD; cd01850; CDC_Septin; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030379; G_SEPTIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016491; Septin.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; GTP-binding; Nucleotide-binding.
FT   CHAIN           1..416
FT                   /note="Cell division control protein 3"
FT                   /id="PRO_0000173495"
FT   DOMAIN          32..307
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          42..49
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          102..105
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          183..186
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          392..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          323..399
FT                   /evidence="ECO:0000255"
FT   BINDING         42..49
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..192
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  47841 MW;  8D300B8B09091ADC CRC64;
     MSTNIKIIKK VLNGYVGFAN LPKQWHRKSI RRGFSLNIMA IGESGLGKAT LINTLFNRDI
     ITSQHDSDEF DEGEEEDVSV KIKSTQAEIE EDGVKLKVSV ITAPGFGESI NNVEAWKPIV
     DEINSRFDSY LEAESRINRT AVVDNRVHAF LYFIEPTGHS LRALDIALMK QVHEKVNLIP
     VIAKSDTLTD EEILEFKHRI LADISHQGIK IFKPTDFEYD EEESANTRSI IDSFPFAVVG
     STNEVQTPDG RLVRGRKYPW GVIEVDNENH NDFVKLRQLL VRNFLEELKE HTANVLYENY
     RTEKLKRMGI EQDNTVFREF DPAAKQEEER ALHEAKLAKM EAEMKSVFQQ KVSEKEKKLQ
     RSEADLFARH KEMKDKLTKQ IKLLEEKKAQ LEKQKLLPQD PPAQPAPQKS RKGFLR