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Database: UniProt
Entry: A0A369GN33_9HYPO
LinkDB: A0A369GN33_9HYPO
Original site: A0A369GN33_9HYPO 
ID   A0A369GN33_9HYPO        Unreviewed;       503 AA.
AC   A0A369GN33;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN   ORFNames=CP532_4968 {ECO:0000313|EMBL:RDA85326.1};
OS   Ophiocordyceps camponoti-leonardi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA85326.1, ECO:0000313|Proteomes:UP000252748};
RN   [1] {ECO:0000313|EMBL:RDA85326.1, ECO:0000313|Proteomes:UP000252748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA85326.1,
RC   ECO:0000313|Proteomes:UP000252748};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) 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:RDA85326.1}.
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DR   EMBL; PDHP01000081; RDA85326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369GN33; -.
DR   STRING; 2039875.A0A369GN33; -.
DR   Proteomes; UP000252748; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   PANTHER; PTHR18884; SEPTIN; 1.
DR   PANTHER; PTHR18884:SF70; SEPTIN; 1.
DR   Pfam; PF00735; Septin; 3.
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|RuleBase:RU004560};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252748}.
FT   DOMAIN          144..500
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..56
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  55949 MW;  06BE280C19C3A175 CRC64;
     MTSSTPRRPS FGMLLRRSKS GDFGKGAAKK KEADLDRHRM NNPPPPPPPP HPPVLPEFRK
     STDQLLSKSF GPELQTAPAY SLSASPSARI SQETPRNFAY PPVPPIPYDV YARTESMTHR
     SRYSYASSAV STINGPRRVR RRKDPTPFNI LIVGTAGAGK TSFLEFLKAA AALPAHKRPS
     KRSEEDDFRL PTMPTGNFVP HYVEAEVDRE RIGLTLWDSE GLEKNVVDLQ LREMLAFVES
     KFEETINEEM KVVRSPGFQD THIHAVLLML DPARLDRNIA TARKLSIGSF SDANGSASGL
     RDLAALDEDV DLQVLRALHG KTTVIPVIAK ADTITAKHMK VLKRAVWSNI KAAGLDPLDA
     LSRNEESDRI DEDDYDSMGS SENGGGGNDD DDDGHIRYSP SGASGGGGSS NESGSTRLSP
     DRNNDDDDKS PLPFSVISPD LYEPGVVGRR FAWGFADPYN EQHCDFQRLK EAVLSDWRTD
     LREASRDRWY EAWRTNRLKH RRR
//
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