ID A0A166BQA3_EXIGL Unreviewed; 382 AA.
AC A0A166BQA3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Septin {ECO:0000313|EMBL:KZW03150.1};
GN ORFNames=EXIGLDRAFT_636301 {ECO:0000313|EMBL:KZW03150.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03150.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW03150.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03150.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR EMBL; KV425884; KZW03150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166BQA3; -.
DR STRING; 1314781.A0A166BQA3; -.
DR InParanoid; A0A166BQA3; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000077266; 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; 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 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:UP000077266}.
FT DOMAIN 25..298
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 347..374
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 382 AA; 44014 MW; 3ABB720F940EE627 CRC64;
MPAPTVAGIG IANLPNQRHK LVAKRGAHFT IMVVGESGLG KTTLINTLFS TELSSSKNYS
RRHVKQLDKL TEVEIIKAEL EEKSFKVKLT VIDTPGFGDY VNNRDSWSPI IDFIDDQHET
YMRQEQQPQR GEKTDLRVHA CLYFIRATGH TLKPLDIEIM KRLGTRVNLI PVIAKADTLT
PSDLANFKER IRATIATQNI RIYRPPIDPE DMQSAEHARL LADAMPFAII GSTEDVQTAD
GRTVKGRQYL WGVAEVENEN HCDFRKLRSL VIRTHMLDLI STTEESHYEN YRQEQMETRK
FGEPKVKKLD NPKFREEEEG LRRRFTEQIK AEDARFRQWE RHLIAERDRL NKDLELAHSA
VKQIEAELDN LQAGYGRGSQ RR
//
