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Database: UniProt
Entry: A0A165J4H2_XYLHT
LinkDB: A0A165J4H2_XYLHT
Original site: A0A165J4H2_XYLHT 
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
//
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