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Database: UniProt
Entry: A0A1Y2GTW6_9FUNG
LinkDB: A0A1Y2GTW6_9FUNG
Original site: A0A1Y2GTW6_9FUNG 
ID   A0A1Y2GTW6_9FUNG        Unreviewed;       425 AA.
AC   A0A1Y2GTW6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Cell division control/GTP binding protein {ECO:0000313|EMBL:ORZ18244.1};
GN   ORFNames=BCR41DRAFT_352022 {ECO:0000313|EMBL:ORZ18244.1};
OS   Lobosporangium transversale.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX   NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ18244.1, ECO:0000313|Proteomes:UP000193648};
RN   [1] {ECO:0000313|EMBL:ORZ18244.1, ECO:0000313|Proteomes:UP000193648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ18244.1,
RC   ECO:0000313|Proteomes:UP000193648};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORZ18244.1}.
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DR   EMBL; MCFF01000015; ORZ18244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2GTW6; -.
DR   STRING; 64571.A0A1Y2GTW6; -.
DR   InParanoid; A0A1Y2GTW6; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000193648; 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   GO; GO:0051301; P:cell division; 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:SF126; 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   Cell cycle {ECO:0000313|EMBL:ORZ18244.1};
KW   Cell division {ECO:0000313|EMBL:ORZ18244.1};
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:UP000193648}.
FT   DOMAIN          47..320
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          392..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  48721 MW;  F009F3488129F819 CRC64;
     MATDIANPIS PPSSNKAAIN GALRKKLQGY VGFANLPNQV HRKSVKKGFN FTIMVVGESG
     LGKSTLVNTL FNAPLYPPKE YAPLTEESPK TVGIQLFSTD IEENGVRLKL NVVDTPGFGD
     FINNEDSWKP ILKTIEGRFD AYLEQENRVN RSKITDTRVN ACLYFIAPTG HSLKALDIEF
     MKRLHNKVNL IPVIAKSDTM THEEIAAFKE RILLDIAHHD IKIYHAQHYD SDDIETINET
     KDVMSKIPFA IVGSDKAIET PDGRHVRGRK YPWGVIEVDN EDHCDFVKLR QMLIRTHMEE
     LKEFTNDIHY ENYRTEKLLA MGYQQDNSVF KEIDPVAKLE EERAMHEAKL IKMEQDMKHV
     FQQKVQEKEA KLTQSEAELY AKHKEMKDAL EKQRLDLEEK KRRIEQGRPI TPEKTKKKGF
     GFAGK
//
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