ID   CDC10_ENCCU             Reviewed;         356 AA.
AC   Q8SQR3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cell division control protein 10;
GN   Name=CDC10; OrderedLocusNames=ECU11_1950;
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=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   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
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; AL590450; CAD26105.2; -; Genomic_DNA.
DR   RefSeq; NP_586501.1; NM_001042334.1.
DR   AlphaFoldDB; Q8SQR3; -.
DR   SMR; Q8SQR3; -.
DR   STRING; 284813.Q8SQR3; -.
DR   GeneID; 860155; -.
DR   KEGG; ecu:ECU11_1950; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_1950; -.
DR   HOGENOM; CLU_017718_8_0_1; -.
DR   InParanoid; Q8SQR3; -.
DR   OrthoDB; 845354at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
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..356
FT                   /note="Cell division control protein 10"
FT                   /id="PRO_0000381760"
FT   DOMAIN          36..286
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          46..53
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          93..96
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          163..166
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   BINDING         46..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..172
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  41331 MW;  B3221C9E86F44C94 CRC64;
     MKNIPTIVRN LGTINIRNNV GFSSVPDQVR ESSMVKGFEL NVLVVGRRGL GTSTLINSIF
     AAPLVDKKRT NNITATRNEI VENDISLEIS IVTYHEANIS PVLDYINAMN REYFDNEQGL
     YKAFKDNRVH VCLYLLPSDT LTDQEIKNMY ELSQSCNLVP IIPKADMYTP DELADVKENV
     RQILSENNIF SFVPYLNEND GDLTEEVADI VGCMPFAVIA SETMYEHGGE IIRGRKYPWG
     FINIDQEESN DFKRLQRLLI YTNLDELTMK TNHLFYNNYR KKIFEIENDC GAMKEARYLR
     LRTETIRILN DKYESRINAL RKEEEEMERF YSEKIREMND KMGEISKQVE KSLHVE