ID A0A397IM93_9EURO Unreviewed; 356 AA.
AC A0A397IM93;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN ORFNames=CDV55_109028 {ECO:0000313|EMBL:RHZ74294.1}, CFD26_105773
GN {ECO:0000313|EMBL:RLM00869.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ74294.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLM00869.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ74294.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-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}.
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:RHZ74294.1}.
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DR EMBL; NKHV02000004; RHZ74294.1; -; Genomic_DNA.
DR EMBL; NIDN02000010; RLM00869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397IM93; -.
DR STRING; 1245748.A0A397IM93; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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; 2.
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; 2.
DR PIRSF; PIRSF006698; Septin; 2.
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:UP000215289}.
FT DOMAIN 1..265
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 290..335
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 356 AA; 40598 MW; 7F401A8D280C5F35 CRC64;
MSSALNAIRR KKNVKKGIQF CLMVCGASGT GRTTFVNTLC GKKVLESKDA DDAASAHIEE
GVRIKPVTVG NFGEIVGYLE RQYDDILAEE SRIKRNPRFR DNRVHVLLYF ITPTGHGLRE
LDIELMKRLS PRVNVIPVIG KADSLTPAEL AESKKLIMED IEHYRIPVYN FPYDIEEDDE
DTVEENAELR GLMPFAIVGS EDFVEIDGRR VRARQYPWGV VEVENPRHSD FLAIRSALLH
SHLADLKEIT HDFLYENYRT EKLSKSVDGA AAYSGHDSSM NPEDLASQSV RLKEEQLRRE
EEKLREIELK VQREIAEKRQ ELLARESQLR EIEARMAREA SQNQMAFQPE ATNGDA
//
