ID   A0A319DIF8_9EURO        Unreviewed;       383 AA.
AC   A0A319DIF8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Septin {ECO:0000313|EMBL:PYH87898.1};
GN   ORFNames=BO71DRAFT_404275 {ECO:0000313|EMBL:PYH87898.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH87898.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH87898.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH87898.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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; KZ826153; PYH87898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DIF8; -.
DR   STRING; 1448320.A0A319DIF8; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProt.
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: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:UP000247810}.
FT   DOMAIN          26..299
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   COILED          316..375
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   383 AA;  44391 MW;  57E75D51C5365E13 CRC64;
     MSSTETASPI GIANLPNQRH KIVAKRGAAF TIMVAGESGL GKTTFINTLF STTIKNYADH
     KRRHQKQVDR TVEIEITKAE LEEKFFKVRL TVIDTPGFGD YVNNRDSWQP IIEFLDDQHE
     SYMLQEQQPR RTDKIDMRVH ACLYFIRPTG HTLKPLDIEV MKRLSSRVNL IPVVAKADTL
     SPSDLARYKQ RIRAVIEAQG IKIYTPPVEE DDEHAATHAR SLMAAMPFAV IGSEKDVKTT
     DNRVVKGRQY AWGVAEVENE DHCDFKKLRS ILIRTHMLDL IHTTEEQHYE VYRAQQMETR
     KFGEARPRKL DNPKFKEEEE NLRKRFTEQV KVEEQRFRQW EQKLIAERDR LNKDLEATHA
     AIKSLEQEID GLQGSSTRSH GRR
//