ID A0A165J4H2_XYLHT Unreviewed; 347 AA.
AC A0A165J4H2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cell division/GTP binding protein {ECO:0000313|EMBL:KZF25719.1};
GN ORFNames=L228DRAFT_244609 {ECO:0000313|EMBL:KZF25719.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF25719.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF25719.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF25719.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(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; KV407455; KZF25719.1; -; Genomic_DNA.
DR RefSeq; XP_018191274.1; XM_018331969.1.
DR AlphaFoldDB; A0A165J4H2; -.
DR STRING; 1328760.A0A165J4H2; -.
DR GeneID; 28897106; -.
DR InParanoid; A0A165J4H2; -.
DR OMA; QCEFVYL; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000076632; 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:SF57; CELL DIVISION CONTROL PROTEIN 10; 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 Cell cycle {ECO:0000313|EMBL:KZF25719.1};
KW Cell division {ECO:0000313|EMBL:KZF25719.1};
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:UP000076632}.
FT DOMAIN 36..308
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 312..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 39328 MW; 66F90B4EEAD0AAEF CRC64;
MAAVNALPSQ PSAVYPNSHV GFDSITSQIE RKLLKRGFQF NVICVGQTGL GKSTLINTIF
ASHLIDSKGR LTPDEHVRST TEIQAASHII EENGVRLRLN IVDTPGYGDQ INNDRCWDPI
VKYIKDQHSA YLRKELTAQR DRYIQDTRIH CCLFFIQPSG HALKPIDIVV LKKLSDVVNV
VPVIAKSDSL TLEERAAFKE RIKEEFSFHN LKMYPYDNDE HDDEERALNS QIKSIIPFAV
VGSEKSIVVN GKQVRGRQNR WGVINVEDEN HCEFIYLRNF LTRTHLQDLI ETTSQIHYET
FRAKQLLALK ESSAAGGHSS RPISPSAERE LSRSSQSNTQ RNTLNGY
//