ID A0A0A1PGZ4_RHIZD Unreviewed; 364 AA.
AC A0A0A1PGZ4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Septin {ECO:0000313|EMBL:ORE14794.1};
GN ORFNames=BCV71DRAFT_220388 {ECO:0000313|EMBL:ORE14794.1};
OS Rhizopus microsporus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE14794.1, ECO:0000313|Proteomes:UP000242381};
RN [1] {ECO:0000313|EMBL:ORE14794.1, ECO:0000313|Proteomes:UP000242381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE14794.1,
RC ECO:0000313|Proteomes:UP000242381};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(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}.
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; KV921452; ORE14794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1PGZ4; -.
DR VEuPathDB; FungiDB:BCV72DRAFT_304829; -.
DR OMA; TNMYLRS; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000242381; 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 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:UP000242381}.
FT DOMAIN 14..289
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 311..363
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 364 AA; 41818 MW; 09D394F4A423FC10 CRC64;
MAHRLGGRRK NVKKGFQFTL MVVGASGTGR TTFVNTLCDA HVLSKKESDN PEDAHKEEGI
NIKPVSVELD EDGVRISLTI VDTPGFGDNI DNEACFHEIV AYLEKQYDDI LAEESRIKRN
PRFRDNRVHA LLYFISPTGH ALREIDIELM RRLSPRVNVI PVIGRADSLT PQELKDFKRR
IMEDIEHYNI PIYNFPYDVE EDDEDTIEEN SELRALLPFS IIGSEEEIVV NGRTVRGRQY
PWGAVEVDNP KHSDFGRLRS ALLSSHLQDL KEITHDILYE NYRTEKLSRT VNGGDQEDAS
LNAEDMATQS VRLKEEQLRK EEEKLREIEL KVQREIQEKR AELLSKEEAL RNLEARLAQA
QLAD
//
