CDC11_ENCCU
ID CDC11_ENCCU Reviewed; 267 AA.
AC Q8STS8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cell division control protein 11;
GN Name=CDC11; OrderedLocusNames=ECU09_0820;
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; AL590451; CAD27055.2; -; Genomic_DNA.
DR RefSeq; XP_955636.1; XM_950543.1.
DR AlphaFoldDB; Q8STS8; -.
DR SMR; Q8STS8; -.
DR STRING; 284813.Q8STS8; -.
DR GeneID; 860421; -.
DR KEGG; ecu:ECU09_0820; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_0820; -.
DR HOGENOM; CLU_017718_7_0_1; -.
DR InParanoid; Q8STS8; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
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 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 1: Evidence at protein level;
KW Cell cycle; Cell division; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..267
FT /note="Cell division control protein 11"
FT /id="PRO_0000381761"
FT DOMAIN 6..263
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 16..23
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 63..66
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 145..148
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 146..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 267 AA; 30239 MW; A809A0AC5C9753BC CRC64;
MIVRRQNRRF TIMAAGPRGS GKSSFFNSLI GKEIVTSRGH EGIDLYMLNL DCEGIMQRIT
LIDTPGFGEG FDDSEIQETI CNFIKAQLDM FIAEESKIRR NPKYEDTRVH CLLYFIPSTS
SSLKSRDIAF LRKVSGLVNI IPVISKSDGL SITERIEVKR QVMEQIKHYN ISIFDLDDPE
VYSSPAAGND LNSLVPFLVV SADRENFESR ARNYQWGDVS IDNPDHCDLP ALRELLLSTH
IYGLIDYTAS EIYENYRAAV LEGGVRK
