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Database: UniProt
Entry: G3AFL6_SPAPN
LinkDB: G3AFL6_SPAPN
Original site: G3AFL6_SPAPN 
ID   G3AFL6_SPAPN            Unreviewed;       444 AA.
AC   G3AFL6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Cell division control protein 3 {ECO:0000313|EMBL:EGW35005.1};
GN   ORFNames=SPAPADRAFT_145753 {ECO:0000313|EMBL:EGW35005.1};
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:EGW35005.1, 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; GL996499; EGW35005.1; -; Genomic_DNA.
DR   RefSeq; XP_007372417.1; XM_007372355.1.
DR   AlphaFoldDB; G3AFL6; -.
DR   STRING; 619300.G3AFL6; -.
DR   GeneID; 18870699; -.
DR   KEGG; spaa:SPAPADRAFT_145753; -.
DR   eggNOG; KOG2655; Eukaryota.
DR   HOGENOM; CLU_017718_8_0_1; -.
DR   InParanoid; G3AFL6; -.
DR   OMA; RSNPMGS; -.
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   GO; GO:0051301; P:cell division; 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   Cell cycle {ECO:0000313|EMBL:EGW35005.1};
KW   Cell division {ECO:0000313|EMBL:EGW35005.1};
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          56..335
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          420..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  50937 MW;  0771192A5041199C CRC64;
     MTSVEPEKQP AIQMPSSVKS PITYTPQDIK IIKKVLNGYV GFANLPKQWH RKSVRRGFTF
     NIMAIGESGL GKATLINTLF NREIVNHRDD EETVEEDTED KEGGVAVKIR STKAEIEEDG
     VKLKVSVITA PGFGESINNT DYWKPIVDEI NSRFDSYLEA ECKINRSTIV DDRIHAFLYF
     IEPTGHSLRA LDIAMMKLVH EKVNLIPIIA KSDTLTDDEI VEFKQRILAD IAHQGIKIFT
     PEAPGDDDEE TVSNTQSIID TFPFAVVGST KEVQTPDGRT VRGRQYPWGV IEVDNEAHND
     FVKLRQLLIR NFLEELKEHT ANVLYENYRT EKLKKMGIEQ DSTVFREFDP LAKQQEERAL
     HEAKLAKMEA EMKSVFQQKV SEKEKKLQRS EADLFARHKE MKDKLTKQIK ILEEKKVQLE
     KQRSLPQEPM VQPAQQKTRK GFLR
//
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