ID C5MFE1_CANTT Unreviewed; 371 AA.
AC C5MFE1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Cell division control protein 12 {ECO:0000313|EMBL:EER32001.1};
GN ORFNames=CTRG_04784 {ECO:0000313|EMBL:EER32001.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32001.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER32001.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000256|ARBA:ARBA00004266}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR EMBL; GG692400; EER32001.1; -; Genomic_DNA.
DR RefSeq; XP_002550486.1; XM_002550440.1.
DR AlphaFoldDB; C5MFE1; -.
DR STRING; 294747.C5MFE1; -.
DR EnsemblFungi; CTRG_04784-t43_1; CTRG_04784-t43_1-p1; CTRG_04784.
DR GeneID; 8296493; -.
DR KEGG; ctp:CTRG_04784; -.
DR VEuPathDB; FungiDB:CTRG_04784; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0005621; C:cellular bud scar; IEA:EnsemblFungi.
DR GO; GO:1990317; C:Gin4 complex; IEA:EnsemblFungi.
DR GO; GO:0005937; C:mating projection; 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:0003924; F:GTPase activity; IEA:EnsemblFungi.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:EnsemblFungi.
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:0030011; P:maintenance of cell polarity; IEA:EnsemblFungi.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:EnsemblFungi.
DR GO; GO:0000921; P:septin ring assembly; IEA:EnsemblFungi.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF109; SEPTIN-1; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:EER32001.1};
KW Cell division {ECO:0000313|EMBL:EER32001.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 1..269
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 269..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 324..369
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 281..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 43018 MW; 6C4F6DEF9B78F079 CRC64;
MVAGESGLGK TTFINTLFQT SLKPHQDPNQ RHNKFTTAHQ TVEIDIVRAI LEEKNFKIRL
NIIDTPGFGN NVNNHDSWVP IIDFIDDQHE SFMKQEQQPS RISKKDLRVH ACLYFIRPTG
HSLKPLDIEI MKKLSTRVNL IPVIAKADTL SPQELDIFKT RIREIIEAQD ISIYTPPLEL
DDTASAEHAK QLIESMPFAV IGSEEEVEVG PGQFVRGRKY PWGVVEVEND QHCDFKKLRS
LLLRTNMLDL ILSTNELHFE TFRSLKLGGE EQETNEENEG AEELTNEKGE VVKKPSNSKK
PRRLHNPKFK EEEDALKKFF TEQVKAEEQR FRQWETNIIN ERNRLNQDLE EMQSKLKTLE
EQVKKLQLAK R
//
