ID A0A420HFH5_9PEZI Unreviewed; 470 AA.
AC A0A420HFH5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Cell division control protein 3 {ECO:0000313|EMBL:RKF56137.1};
GN ORFNames=OnM2_083047 {ECO:0000313|EMBL:RKF56137.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF56137.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF56137.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF56137.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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:RKF56137.1}.
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DR EMBL; MCFK01008380; RKF56137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420HFH5; -.
DR STRING; 212602.A0A420HFH5; -.
DR Proteomes; UP000286134; 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:RKF56137.1};
KW Cell division {ECO:0000313|EMBL:RKF56137.1};
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:UP000286134}.
FT DOMAIN 95..368
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 53272 MW; 5691D58A2372A5D4 CRC64;
MAGANKAVVE ANVGSPMAPS RASPSPPTSS NGAFAMGETL SRTNGQPHAP QTVSAKNPKA
AAAMANDMNI VRRKLTGYVG FANLPNQWHR KSVRKGFNFN VMVVGESGLG KSTLVNTLFN
TSLYPPKERK PPSLDISKTV SVQSISADTE ENGVRLRLTV VDTPGFGDFI NNDESWDPIV
KNIEQRFDAY LEAENKVNRM NVVYNRIHAV VYFIQPTGHS LKPLDIEVMK KLHTKVNLIP
VIAKADTVTD DDLDNYKIRI LADIAHHKIQ IFEGPRYELD DEETIAENQE IMSKVPIAVV
GSNTEVTTPD GRTVRGRQLP WGVVEVDNEE HCDFVKLRQM LIRTHMEELK ENTNNALYEN
YRSEKLTSMG VQQDSTVFKE INPAVKQEEE RSLHEQKLQK MEMKMKMVFQ QKVQEKESKL
RQSDEELYAR HKEMKDQLDR QRQELEEKKS RVESGRPIEE KGKRKGFSLR
//
