ID   Q6BVJ0_DEBHA            Unreviewed;       590 AA.
AC   Q6BVJ0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   24-JAN-2024, entry version 112.
DE   SubName: Full=DEHA2C02266p {ECO:0000313|EMBL:CAG85817.2};
GN   OrderedLocusNames=DEHA2C02266g {ECO:0000313|EMBL:CAG85817.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG85817.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG85817.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
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; CR382135; CAG85817.2; -; Genomic_DNA.
DR   RefSeq; XP_457779.2; XM_457779.1.
DR   AlphaFoldDB; Q6BVJ0; -.
DR   STRING; 284592.Q6BVJ0; -.
DR   GeneID; 2900673; -.
DR   KEGG; dha:DEHA2C02266g; -.
DR   VEuPathDB; FungiDB:DEHA2C02266g; -.
DR   eggNOG; KOG2655; Eukaryota.
DR   HOGENOM; CLU_017718_7_4_1; -.
DR   InParanoid; Q6BVJ0; -.
DR   OMA; IQECKFL; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
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:SF84; SEVENTH HOMOLOG OF 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   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:UP000000599}.
FT   DOMAIN          27..345
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  67487 MW;  198B84C26323C26C CRC64;
     MDQSYTFDSP SMTSHSPMIN YRKDAKKGVK FTFMVVGEMG TGKTTFVNSL LNKKVMSHRY
     EENNGQQYDT KTLSFTSAKS IALPNTAVLT RNDFNPSTAN EEPGIALTET KVEMVDDDNM
     KLYLNIIDTP GFGENLNNEI CFVEIENYLK QQFDLVLAEE TRIRRNPRFV DTRVHVMLYF
     ITATGHGLRE IDINCMKRLS KYVNILPVIS KADTFTETEL RHFKQQVKID IEKFNVPIFQ
     FDNSLSEYDE EDDYELIQEC KYLSSLQPFA IISSEDEYEI TDPRTGESKI TKARQYPWGL
     VDINNPKYSD FGTLKSVLLG THLQDFKDLT HDFLYETYRT ERLSKVTGRI DDEDDDREFH
     ESYEEQPYED SFLKDTTTIP SLSNLAQLTS SNPLHGFGDD HSITSTSSSK ANNKSMLLDG
     TEPSSGMPSP KLRDNASTSS RSTISVENGH QTRNLNSNNA AFKRLSIAPQ RNQLRQISET
     VPYVIRHERI LERQQKLEEM EMASAKELSS RAALLEQKAA ALKAKERLMM KKSETERLRH
     VGGDSSDAVS QRSQQYHYDN EDDLNNSEAN YSVIQKEETL TDLHSIVSQK
//