ID A0A317XD15_9EURO Unreviewed; 375 AA.
AC A0A317XD15;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Septin {ECO:0000313|EMBL:PWY96506.1};
GN ORFNames=BO94DRAFT_505811 {ECO:0000313|EMBL:PWY96506.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY96506.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY96506.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY96506.1,
RC ECO:0000313|Proteomes:UP000246702};
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 (DEC-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY96506.1}.
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DR EMBL; MSFK01000001; PWY96506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XD15; -.
DR STRING; 1450535.A0A317XD15; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000246702; 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: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 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:UP000246702}.
FT DOMAIN 11..288
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 288..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 42777 MW; 16E95D0407A110F2 CRC64;
MKLRRKKNVK KGIQFCLMVC GASGTGRTTF VNTLCGKKVL EGKDSDDPAN AHIEEGVRIK
PVTVELELDD EGTRISLTIV DTPGFGDQID NEASFGEIVG YLERQYDDIL AEESRIKRNP
RFRDNRVHVL LYFITPTGHG LRELDIELMK RLSPRVNVIP VIGKADSLTP AELAESKKLI
MEDIEHYRIP VYNFPYDIEE DDEDTVEENA ELRGLMPFAI VGSEDFVEID GKKVRARQYP
WGVVDVENPR HSDFLAIRSA LLHSHLADLK EITHDFLYEN YRTEKLSKSV DGATPHSTQD
SSMNPEDLAS QSVRLKEEQL RREEEKLREI ELKVQREIAE KRQELLARES QLREIEARMA
REASQSQVDS TNGDA
//
