ID A0A0D7A2T8_9AGAR Unreviewed; 383 AA.
AC A0A0D7A2T8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Septin {ECO:0000313|EMBL:KIY44694.1};
GN ORFNames=FISHEDRAFT_50834 {ECO:0000313|EMBL:KIY44694.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY44694.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY44694.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY44694.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN882067; KIY44694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7A2T8; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000054144; 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:UP000054144}.
FT DOMAIN 25..297
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 314..366
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 383 AA; 44253 MW; 44F853FE61E08CC6 CRC64;
MSFPQVDGIG IANLPNQRHK IVAKRGAHFT IMVVGESGLG KTTLINTLFS TELSPAKNYS
RRHTKIADKL TEVEIIKAEL EEKQFKVKLT VIDTPGFGDY VNNRDSWSPI VDFIDDQHEA
YMRQEQQPQR HEKTDLRVHA CLYFIRPTGH TLKPLDIEIM KRLGTRVNLI PVIAKADTLT
QNDLFTFKQR IREVIAAQGI RIYTPPIEAD DESAESARIL TDAMPFSIIG STEDVKTPDG
RVAKGREYLW GVAEVENENH CDFKKLRSLL IRTHMLDLIS TTEESHYENY RQQQMETRKF
GEPKVKKLDN PKFREEEEQL RKKFTDQVKA EEARFRQWEQ HLIAERDRLN KDLEVAHSAI
KQLEVELDNL GMGPHIRGTS NRR
//
