CDC10_CANAL
ID CDC10_CANAL Reviewed; 357 AA.
AC P39827; A0A1D8PSR7; Q5A6K6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cell division control protein 10;
GN Name=CDC10; OrderedLocusNames=CAALFM_CR04570CA;
GN ORFNames=CaO19.548, CaO19.8183;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 -!- DEVELOPMENTAL STAGE: Expressed at higher levels in cells growing as
CC hyphae than in those growing as budding yeasts.
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; Z25870; CAA81090.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW31193.1; -; Genomic_DNA.
DR PIR; S43278; S43278.
DR RefSeq; XP_717411.2; XM_712318.2.
DR AlphaFoldDB; P39827; -.
DR SMR; P39827; -.
DR BioGRID; 1223999; 7.
DR STRING; 237561.P39827; -.
DR PRIDE; P39827; -.
DR GeneID; 3640947; -.
DR KEGG; cal:CAALFM_CR04570CA; -.
DR CGD; CAL0000188354; CDC10.
DR VEuPathDB; FungiDB:CR_04570C_A; -.
DR eggNOG; KOG1547; Eukaryota.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; P39827; -.
DR OMA; QCEFVYL; -.
DR OrthoDB; 845354at2759; -.
DR PHI-base; PHI:281; -.
DR PRO; PR:P39827; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005938; C:cell cortex; IDA:CGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IDA:CGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:CGD.
DR GO; GO:1990317; C:Gin4 complex; IEA:EnsemblFungi.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:CGD.
DR GO; GO:0001400; C:mating projection base; IEA:EnsemblFungi.
DR GO; GO:0032175; C:mating projection septin ring; IEA:EnsemblFungi.
DR GO; GO:0036391; C:medial cortex septin ring; IEA:EnsemblFungi.
DR GO; GO:0032152; C:meiotic septin complex; IEA:EnsemblFungi.
DR GO; GO:0072687; C:meiotic spindle; IEA:EnsemblFungi.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IEA:EnsemblFungi.
DR GO; GO:0032151; C:mitotic septin complex; IEA:EnsemblFungi.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0032169; C:prospore septin ring; IEA:EnsemblFungi.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0032160; C:septin filament array; IEA:EnsemblFungi.
DR GO; GO:0005940; C:septin ring; IDA:CGD.
DR GO; GO:0005876; C:spindle microtubule; IEA:EnsemblFungi.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
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:0044406; P:adhesion of symbiont to host; IMP:CGD.
DR GO; GO:0006033; P:chitin localization; IMP:CGD.
DR GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0010458; P:exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0070783; P:growth of unicellular organism as a thread of attached cells; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0007097; P:nuclear migration; IMP:CGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:EnsemblFungi.
DR GO; GO:0008104; P:protein localization; IMP:CGD.
DR GO; GO:0000921; P:septin ring assembly; IMP:CGD.
DR GO; GO:0070583; P:spore membrane bending pathway; 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 2: Evidence at transcript level;
KW Cell cycle; Cell division; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..357
FT /note="Cell division control protein 10"
FT /id="PRO_0000173497"
FT DOMAIN 34..306
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 44..51
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
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 310..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104
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 255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 338
FT /note="T -> A (in Ref. 1; CAA81090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40684 MW; 7C25CC98376749E2 CRC64;
MSIEEPSTQH IAQPQKYVGF DTITTQIENR LLKRGFQFNI MVVGRSGLGK STLVNTLFSS
KLTTSQGRKS PSEPIEKTTE IKVASHSLLE NNVRLNINVI DTPGFGDQIN NEKCWEPLVK
YVKEQHSQYL RKELTAQRDK FLADTRVHCI LYFIPPNGQK LKQLDVQALK KLSEIANVVP
IIAKSDSLTL DERSEFKKLL QSEFMKYNFN IYPYDSEDLY EEERQLNEDI KSLIPFAIAG
SETEIEINGE MVRGRKTKWG AINIEDVSQC EFVFLRDFLT RTHLQDLIET TALTHYETFR
SKQLIALKEN ASNPNRQSQL QKDQGQTSQQ SNQDLKNTSG VPNAPMFQST TGTAAAR
