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Database: UniProt
Entry: H8X1X5_CANO9
LinkDB: H8X1X5_CANO9
Original site: H8X1X5_CANO9 
ID   H8X1X5_CANO9            Unreviewed;       447 AA.
AC   H8X1X5;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Cdc3 septin {ECO:0000313|EMBL:CCG22531.1};
GN   ORFNames=CORT_0B08260 {ECO:0000313|EMBL:CCG22531.1};
OS   Candida orthopsilosis (strain 90-125) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG22531.1, ECO:0000313|Proteomes:UP000005018};
RN   [1] {ECO:0000313|EMBL:CCG22531.1, ECO:0000313|Proteomes:UP000005018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX   PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA   Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT   "Sequence and analysis of the genome of the pathogenic yeast Candida
RT   orthopsilosis.";
RL   PLoS ONE 7:e35750-e35750(2012).
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; HE681720; CCG22531.1; -; Genomic_DNA.
DR   RefSeq; XP_003867967.1; XM_003867919.1.
DR   AlphaFoldDB; H8X1X5; -.
DR   GeneID; 14539035; -.
DR   KEGG; cot:CORT_0B08260; -.
DR   eggNOG; KOG2655; Eukaryota.
DR   HOGENOM; CLU_017718_8_0_1; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000005018; Chromosome 2.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:UniProt.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:SF126; SEPTIN; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004560}.
FT   DOMAIN          46..338
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          423..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  51127 MW;  1AECF42DB3EF0D5A CRC64;
     MTSVVDHSHA PLSSTSQNIK IIKRVLNGYV GFANLPKQWH RRSLRRGFAL NIMAVGEAGL
     GKATLINTLF NRDIMGKSSG NKLNDFDEDQ DEDFADAEVE PSEKEADTGV RIKSTEAEIE
     EDGVKLKVSV ITAPGFGEAL NNIDSWKPIV DEINNRFDSY LEAESRINRS TIVDNRVHAF
     LYFIEPTGHS LRSLDIALMK QVHEKVNLIP IISKSDTLTD EEVHEFKHAI LADIEHHGIK
     IFTPSVSEND DEEVIANTTQ LLKTFPFAVI GSMNEVQTGD GRLVRGRRYP WGVIEVDNED
     HNDFVKLREL LVRNFLEELK ETTSNVLYEH YRTEKLRKMG IEQDNSVFKE FDPATKQEEE
     RALHEAKLAK MEQEMKAVFQ QKVSEKEKKL QRSEADLFAR HKEMKDKLTK QIKLLEDKKV
     QLEKQKLLPQ EPSPQPAPQK SRKGFLR
//
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