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Database: UniProt
Entry: A0A369H4N1_9HYPO
LinkDB: A0A369H4N1_9HYPO
Original site: A0A369H4N1_9HYPO 
ID   A0A369H4N1_9HYPO        Unreviewed;       403 AA.
AC   A0A369H4N1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-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=CP533_2680 {ECO:0000313|EMBL:RDA89993.1};
OS   Ophiocordyceps camponoti-saundersi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA89993.1, ECO:0000313|Proteomes:UP000253071};
RN   [1] {ECO:0000313|EMBL:RDA89993.1, ECO:0000313|Proteomes:UP000253071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA89993.1,
RC   ECO:0000313|Proteomes:UP000253071};
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:RDA89993.1}.
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DR   EMBL; PDHQ01000222; RDA89993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369H4N1; -.
DR   STRING; 2039874.A0A369H4N1; -.
DR   Proteomes; UP000253071; 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; 2.
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:UP000253071}.
FT   DOMAIN          28..319
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   COILED          336..395
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   403 AA;  46336 MW;  0800E305E5BAF4FF CRC64;
     MAPPAPESAS PIGIANLPNQ RHKIVAKRGA SFTIMVAGES GLGKTTFINT LFSTTIKNYA
     DHKRRHQKQV DKTVEIEITK AELEEKFFKG TASSPLPSMA ATDQFFTVRL TVIDTPGFGD
     YVNNRDSWMP IIEFLDDQHE SYMLQEQQPR RQDKIDLRVH ACLYFIRPTG HTLKPLDIEV
     MKRLCSRVNL IPVIAKADTL SSADLAKFKE RIINVIEAQN IKIYQPPIEE DDEAAAQHAR
     SLMAAMPFAV IGSEKDVKTG DGRIVKGRQY SWGVAEVENE DHCDFKKLRS ILIRTHMLDL
     IHTTEELHYE AYRAQQMETR KFGEARPRKL DNPKFKEEEE ALRKRFTEQV KIEEQRFRQW
     EQKLIAERDR LNKDLEQTHA QIKQLEGELE AMQGSAVRSH GRR
//
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