ID   CDC3_ENCCU              Reviewed;         371 AA.
AC   Q8SSI8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cell division control protein 3;
GN   Name=CDC3; OrderedLocusNames=ECU01_1370;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11157783; DOI=10.1101/gr.164301;
RA   Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA   Weissenbach J., Saurin W., Vivares C.P.;
RT   "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT   parasite Encephalitozoon cuniculi (Microspora).";
RL   Genome Res. 11:198-207(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Septins are GTPases involved in cytokinesis. The septins
CC       localize to the site of cleavage and act as a structural scaffold that
CC       recruits different components involved in diverse processes at specific
CC       stages during the cell cycle. Septins are also involved in cell
CC       morphogenesis, chitin deposition, cell cycle regulation, cell
CC       compartmentalization and spore wall formation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the septin complex. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
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; AL391737; CAD25010.1; -; Genomic_DNA.
DR   RefSeq; XP_965975.1; XM_960882.1.
DR   AlphaFoldDB; Q8SSI8; -.
DR   SMR; Q8SSI8; -.
DR   STRING; 284813.Q8SSI8; -.
DR   GeneID; 860316; -.
DR   KEGG; ecu:ECU01_1370; -.
DR   VEuPathDB; MicrosporidiaDB:ECU01_1370; -.
DR   HOGENOM; CLU_017718_8_0_1; -.
DR   InParanoid; Q8SSI8; -.
DR   OMA; AKFKRNI; -.
DR   OrthoDB; 845354at2759; -.
DR   Proteomes; UP000000819; Chromosome I.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:UniProt.
DR   GO; GO:0005525; F:GTP 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   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   1: Evidence at protein level;
KW   Cell cycle; Cell division; GTP-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..371
FT                   /note="Cell division control protein 3"
FT                   /id="PRO_0000381762"
FT   DOMAIN          22..307
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          32..39
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          113..116
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          194..197
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   BINDING         32..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..203
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  42680 MW;  53991973A6DEA33D CRC64;
     MAQKGIGVSN LPNVKYRSFC KAGIDFNIMT VGSNGLGKSS FINQMLGDSI LSSDPFLKPE
     DGHHSNETVR ALDEDIVDDP ESKYFHRNSL INIQISKFFV MENDFQTRVT VTEVDGVGDG
     VCNEGCWDPI VELIQDNFRD YLDQERKNVR SLIKDKRIHI CLYFLEPNPS HVSLVDIRTM
     KEISKICNLI PVVGKSDLLS DSEREECRNR IVEVLSMENI DVFRLDILEK EKISRTESPF
     FIIAKNVNSG DSSGHNREYP WGTMFPEKVE SNDFYFLVDS LIAKNLIRLV ETTEVFYDEY
     KTREIGLSIA SKPGALGEDD RRLTKEIQKK IKEDERTIVE LRQKLIEKRK YYESKMLEIT
     SKYSNEKINS S