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Database: UniProt
Entry: A0A0L1J870_ASPNO
LinkDB: A0A0L1J870_ASPNO
Original site: A0A0L1J870_ASPNO 
ID   A0A0L1J870_ASPNO        Unreviewed;       386 AA.
AC   A0A0L1J870;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Septin spn3 {ECO:0000313|EMBL:KNG87996.1};
GN   ORFNames=ANOM_004558 {ECO:0000313|EMBL:KNG87996.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG87996.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG87996.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG87996.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) 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:KNG87996.1}.
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DR   EMBL; JNOM01000064; KNG87996.1; -; Genomic_DNA.
DR   RefSeq; XP_015408919.1; XM_015549815.1.
DR   AlphaFoldDB; A0A0L1J870; -.
DR   STRING; 1509407.A0A0L1J870; -.
DR   GeneID; 26806362; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000037505; 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:UP000037505}.
FT   DOMAIN          18..303
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          303..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  43795 MW;  8647B021B010C98B CRC64;
     MSSAFNAIKL RRKKNVKKGI QFCLMVCGAS GTGRTTFVNT LCGKQVLEGK DADDAANAHV
     EEGVRIKPVT VELELDDEGT RISLTIVDTP GFGDQIDNEA RHVNAASASF GEIVGYLERQ
     YDDILAEESR IKRNPRFRDN RVHVLLYFIT PTGHGLRELD IELMKRLSPR VNVIPVIGKA
     DSLTPAELAE SKKLIMEDIE HYRIPVYNFP YDIEEDDEDT VEENAELRGL MPFAIVGSDD
     FVEIDGRKVR ARQYPWGVVE VENPRHSDFL AIRSALLHSH LADLKEITHD FLYENYRTEK
     LSKSVDGVSS AQDSSMNPED LASQSVRLKE EQLRREEEKL REIELRVQRE IAEKRQELLA
     RESQLREIEA RMARESSSQD VANGDA
//
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