ID A0A395MUC4_9HYPO Unreviewed; 678 AA.
AC A0A395MUC4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=6-phosphofructo-2-kinase {ECO:0000313|EMBL:RFN51548.1};
GN ORFNames=FIE12Z_4174 {ECO:0000313|EMBL:RFN51548.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN51548.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN51548.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN51548.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(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:RFN51548.1}.
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DR EMBL; PXXK01000099; RFN51548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MUC4; -.
DR STRING; 2594813.A0A395MUC4; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
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 InterPro; IPR001345; PG/BPGM_mutase_AS.
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 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.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RFN51548.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Transferase {ECO:0000313|EMBL:RFN51548.1}.
FT DOMAIN 146..212
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 252..419
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 75995 MW; 5587418E8D095F5E CRC64;
MQNLLGASPP SPALPARNSA APTSSNSLPP TSNPSSNPTP NPTSDPSSHP NNPNNYAVLP
PPPDGDHDHL PPPANAPSSL AVALRSLNDL TETPTYARSV TSTAPSSPRI PPLRQNSGGH
TPRVRPHATT LNIPGMTRSR VSPDGKISSR DVAAKLVIVM VGLPARGKSY ITKKLQRYLS
WQQHDSRIFN VGNRRRTAAG RRVSVHPKLQ AEQEHMDPPV HAASILLNGN PAPFGPDSSE
PEKLDLNDAS QSEVDQSATF FDPKNQTAAA MREQCAMDTL DELLDYLLDQ GGAVGILDAT
NSTIERRMNI AKRVKQREPK LGILFIESIC QDPNLLEANM RLKLSGPDYR DKDPQKSLED
FKKRVAAYES AYVPLGEYEE KNDLQYIQMV DVGRKLIQHR LKGFLSSGIS TYLASFNLAP
RQIWITRHGQ SVDNEIGRLG GNSALTERGH CYGQALHNFI TYQRKQWCME QKSKKAQASF
PPIPGDNTPP YPELNREIED KNFCVWTSML DRSVETAEYF EADDDYDVKN WEMLNEMNSG
QFEGWTYAEI AKKEPEEFAK RAHDKLNYIY PGVGGEGYLQ VVSRLRDMVR EVERIEDHLL
IIGHRSVCRV LMAYFMDLSL ADITDMDIPL GMLYSIEPKP YGLDFHAYRY NEDQGWFEEL
PNYRPQKTAR NSIIKPQH
//
