ID A0A369HJB3_9HYPO Unreviewed; 464 AA.
AC A0A369HJB3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
DE Flags: Fragment;
GN ORFNames=CP533_3467 {ECO:0000313|EMBL:RDA95312.1};
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:RDA95312.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA95312.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA95312.1,
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:RDA95312.1}.
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DR EMBL; PDHQ01000006; RDA95312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369HJB3; -.
DR STRING; 2039874.A0A369HJB3; -.
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:SF123; CELL DIVISION CONTROL PROTEIN 11; 1.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR Pfam; PF00735; 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:UP000253071}.
FT DOMAIN 98..375
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 376..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDA95312.1"
SQ SEQUENCE 464 AA; 52158 MW; A5F2E5B7A3A8CE78 CRC64;
TIPATTTASL APFRPLHPFP LLPPAPSLLL YRNLIPTVVF SHSPPNSEAL LRHRTPLCSS
ILLLCSAQDA FTTARRLAIP ATMSSPAKML RRKKNVKKGI QFCLMVCGAS GTGRTTFVNT
LCGKDVLQHK DSDDAADAHV EDGVKIKPVT VELELDEEGT RISLTIVDTP GFGDQIDNEA
SFAEIVGYLE RQYDDILAEE SRIKRNPRFR DNRVHAMLYF ITPTGHGLRE LDIELMKRLA
PRVNVIPVIG RSDTLTPAEL AESKKLVMED IEHYRIPVYN FPYDIEEDDE DTVEENAELR
GLMPFAIVGS EDAVDIGGRK VRARQYPWGT VEVDNPRHSD FLAIRSALLH SHLADLKEIT
HDFLYENYRT EKLSKSVDGA SGNADSSMNP EDLASQSVRL KEEQLRREEE KLREIELKVQ
REINEKRQEL LARESQLREI EARMQREATQ STTPAPDANG ETAE
//
