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Database: UniProt
Entry: G3AN63_SPAPN
LinkDB: G3AN63_SPAPN
Original site: G3AN63_SPAPN 
ID   G3AN63_SPAPN            Unreviewed;       389 AA.
AC   G3AN63;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN   ORFNames=SPAPADRAFT_138729 {ECO:0000313|EMBL:EGW31906.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW31906.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996502; EGW31906.1; -; Genomic_DNA.
DR   RefSeq; XP_007375182.1; XM_007375120.1.
DR   AlphaFoldDB; G3AN63; -.
DR   STRING; 619300.G3AN63; -.
DR   GeneID; 18870145; -.
DR   KEGG; spaa:SPAPADRAFT_138729; -.
DR   eggNOG; KOG2655; Eukaryota.
DR   HOGENOM; CLU_017718_7_4_1; -.
DR   InParanoid; G3AN63; -.
DR   OMA; TNMYLRS; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
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:SF123; CELL DIVISION CONTROL PROTEIN 11; 1.
DR   PANTHER; PTHR18884; 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   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:UP000000709}.
FT   DOMAIN          22..303
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   COILED          334..383
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   389 AA;  44792 MW;  934C8B97BF7E4B27 CRC64;
     MATFDQANSS TSALRKRKTL KKSINFSIMI VGESGMGRST LINTLCGGTS SIVPTSSTIN
     QDPFTKKLSL RHENVELEDN EGHKISLNII DTPNFANSIN CSEDFKIIVD FIRHQFDEVL
     LEESRVRRNP RFKDGRIHVL IYMINPTSHG LSAIDKKLLL SVNHLVNIIP VIAKADSLTP
     AELQLNKQLI LEDLNQYGIN FYKFNEYEYE QDYIDEEIIE YNKYLNSLTP FAIIGANEIK
     EDQGEQLKFR LLGKNMVPIN VENPDLNDFT ILKNVLLITH LNEFKDLTHD VIYENYRTEA
     LSGKQFQYAE EEEASSPIPD PDIDTSITPE APNYLLKEEQ IKLEEERLKK FEERVHQDLI
     NKRKELLEKE MELKEIEKRL KAEGVTLDS
//
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