ID A0A420I550_9PEZI Unreviewed; 669 AA.
AC A0A420I550;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Putative 6-phosphofructo-2-kinase PB17E12.14c {ECO:0000313|EMBL:RKF64786.1};
GN ORFNames=OnM2_016058 {ECO:0000313|EMBL:RKF64786.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF64786.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF64786.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF64786.1};
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 -!- 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:RKF64786.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFK01001632; RKF64786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420I550; -.
DR STRING; 212602.A0A420I550; -.
DR Proteomes; UP000286134; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10606:SF32; 6-PHOSPHOFRUCTO-2-KINASE 1; 1.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR Pfam; PF01591; 6PF2K; 2.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RKF64786.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000286134};
KW Transferase {ECO:0000313|EMBL:RKF64786.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 399..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..217
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 256..422
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 22..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 669 AA; 76651 MW; 2BDC906ABB14A372 CRC64;
MDNPIVNRHC TQFMSIKKND ASSFPLQNYP SPQDFENKYQ QTHHHHHQDS FQQYQKSLLP
QNNTLERHQQ KNSYHPTTSS QISKHKSASC TTKNMKNCSS PNSGDVFTTS APSSPKIKPT
RHSSGTTTPR VRPPATTLNI PGMTRSKISP DGKISQKDVG AKLVVIMVGL PARGKSYITK
KIQRYLSWQQ HSTKIFNVGN RRRIVAGSSE WGSQKQYQSL HNSTMDPPTQ AAHMLLNGID
PLQYKTNSEL HAINNTMEQS AEFFDPKNEQ ASQFRDQVAL ATLDELLDFL LLENGSVGIL
DATNSTIERR KALFKHIKNR EPKLNILFIE SVCRDEKLLE ANMYLKLRGP DYRGKDPQKS
LADFKKRVAA YGSAYVPLGD YEEENGMQYI KMIDVGRKII HFGLQGFLAF GIAAYLFTFN
LSPRQIWITR HGKSVDNTLG KIGGDSDLTE DGEHFATALY NFVDKKRHQW EMDQKNRALN
SMKLPQPGDQ SPPYPDLLGE LETKNFCIWT SMLKRSIRTA KEFCDDDNYD AKHWEMLNEM
HAGSFEGLTD EFIASNYPEE YAKRAMDRLG YIYPGVGGEG YLQLISRLRD MVREIERIKD
HVLIIGHRSV CRILMAYFMD LQREAISDLE IPLGMLFSIE PKPYGIEFHA YKYNEDTFDF
DEIKDYKYC
//
