ID Q6C7L3_YARLI Unreviewed; 381 AA.
AC Q6C7L3;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 24-JAN-2024, entry version 113.
DE SubName: Full=YALI0D27148p {ECO:0000313|EMBL:CAG81555.2};
GN ORFNames=YALI0_D27148g {ECO:0000313|EMBL:CAG81555.2};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG81555.2, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG81555.2, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382130; CAG81555.2; -; Genomic_DNA.
DR RefSeq; XP_503349.2; XM_503349.2.
DR AlphaFoldDB; Q6C7L3; -.
DR STRING; 284591.Q6C7L3; -.
DR EnsemblFungi; CAG81555; CAG81555; YALI0_D27148g.
DR GeneID; 2910295; -.
DR KEGG; yli:YALI0D27148g; -.
DR VEuPathDB; FungiDB:YALI0_D27148g; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q6C7L3; -.
DR OMA; EASHAEI; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
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:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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; IBA:GO_Central.
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:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
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 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:UP000001300}.
FT DOMAIN 28..301
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 350..377
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 381 AA; 44025 MW; 8FE1915DE91D1650 CRC64;
MATTAQAAIQ SIGVANLPNQ RHKIVAKSGA TFTLMVAGES GLGKTTFVNT LFSTSIKSYT
DNKTRFKRPI KKTVEIDVTK AELEERGFRV RLNVIDTPGF GDNVNNLDSW QPIVEFLDDQ
HESFMRQEQQ PNRVGKIDMR VHACIYFIRP TGHGLKPLDI EAMKKLSSRV NLIPVIAKAD
TLSRKELAIF KQRVRDTIIA QNIRIYQPSV DEEDQRAAEH AKSLIDAMPY SIIASEKDVE
TPDGRVVKGR QYLWGVAEVE NEDHCDFEKL RYLLIRTHML DLTASTEELH YESYRTQQME
TRKFGEARPR KFDNPKFKEE EDALRKMFTE QVKLEEQRFR QWEQNLIAER DRLNKDLEQT
HASIRALEQE VEQLTMKAGK R
//
