ID A0A0M8N3U8_9HYPO Unreviewed; 609 AA.
AC A0A0M8N3U8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=6-phosphofructo-2-kinase 1 {ECO:0000313|EMBL:KOS22627.1};
GN ORFNames=ESCO_001748 {ECO:0000313|EMBL:KOS22627.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS22627.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS22627.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS22627.1}.
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DR EMBL; LGSR01000006; KOS22627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N3U8; -.
DR STRING; 150374.A0A0M8N3U8; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000053831; 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; 2.
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.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KOS22627.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Transferase {ECO:0000313|EMBL:KOS22627.1}.
FT DOMAIN 78..141
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 188..354
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 68900 MW; A953204F441D9600 CRC64;
MIDFGDSSSF SRSVSTTASS SPRIVIGGSA QYQDQFHPPL RQNSGSQTPR VRPHATTLNI
PGMTRSKVSP DGRIPQRDVA AKLVIVMVGL PARGKSYITK KLQRYLSWQQ HESRIFNVGN
RRRNAVSISV PGSSRTSAQK QQQQQEDAAS PVRAASILLN GAPADNGAFD RDESPDFDRK
HNNPEASKEV DQSAQFFDPK NEKAAAFREQ VAMDTLDELL DYMLIGGGAV GILDATNSTI
ERRQHVVDHI KSREPKLGIL FIESICTDPT LLEANMRLKL SGPDYRDKDP VKSLEDFKAR
VAAYESAYVP LGKYEEDNDM QYIQMIDVGR KLVQHRLKGF LSGGISNYLS SFNLAPRQIW
ITRHGQSVDN ELGRLGGDSP LTERGHCYAQ ALHTFITHKR REWLVEQKSV LARASFPPLP
GDNTPPYPDM YHDLDDKNFC VWTSMLGRSV ETAEYFDVDD DYDVKNWEML NEMNSGTFEG
MTYDEIAMRF PDEFLKRAKD KLNYIYPGVG GEGYLQVISR LRTMVREIER IDDHLLIIGH
RSVCRVLMAY FMDLTREDIT DMDIPLGMLY SIEPKPYGIA FHAYRYNESL GWFDELPNYK
PQKAARGSV
//
