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Database: UniProt
Entry: A0A0B1NWW3_UNCNE
LinkDB: A0A0B1NWW3_UNCNE
Original site: A0A0B1NWW3_UNCNE 
ID   A0A0B1NWW3_UNCNE        Unreviewed;       382 AA.
AC   A0A0B1NWW3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative sporulation-regulated protein {ECO:0000313|EMBL:KHJ30827.1};
GN   ORFNames=EV44_g0368 {ECO:0000313|EMBL:KHJ30827.1};
OS   Uncinula necator (Grape powdery mildew).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ30827.1, ECO:0000313|Proteomes:UP000030854};
RN   [1] {ECO:0000313|EMBL:KHJ30827.1, ECO:0000313|Proteomes:UP000030854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX   PubMed=25487071;
RA   Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA   Walker M.A., Cantu D.;
RT   "Adaptive genomic structural variation in the grape powdery mildew
RT   pathogen, Erysiphe necator.";
RL   BMC Genomics 15:1081-1081(2014).
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:KHJ30827.1}.
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DR   EMBL; JNVN01003553; KHJ30827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1NWW3; -.
DR   STRING; 52586.A0A0B1NWW3; -.
DR   HOGENOM; CLU_017718_7_4_1; -.
DR   OMA; TNMYLRS; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000030854; 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   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:UP000030854}.
FT   DOMAIN          18..295
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          294..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  43389 MW;  B10BD196EED09D45 CRC64;
     MSSPLSAIKI RRKKNVKKGI QFCLMVCGAS GTGRTTFVNT LCGKKVLAGK DADDAANAHV
     EEGVRIRPIT VELELDEEGT RISLTIVDTP GFGDQIDNEA SFGEIVGYLE RQYDDILAEE
     SRIKRNPRFR DNRVHALLYF ITPTGHGLRE LDIELMKRLS PRVNVIPVIG KADSLTPAEL
     AESKKLVMED IEHYRIPVYN FPYDIEEDDE DTVEENAELR GLMPFAIVGS EETVEIAGRK
     VRARQYPWGV VEVDNPRHSD FLAIRSALLH SHLADLKEIT HDFLYENYRT EKLSKSVEGG
     TGTESTMNPE DLASQSVRLK EEQLRREEEK LREIEVKVQR EINEKRQELL ARESQLKEIE
     ARMQREQSSH LELTNGGTEM EG
//
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